Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5KAF

RT XFEL structure of Photosystem II in the dark state at 3.0 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0009055	molecular_function	electron transfer activity
A	0009523	cellular_component	photosystem II
A	0009635	biological_process	response to herbicide
A	0009772	biological_process	photosynthetic electron transport in photosystem II
A	0010242	molecular_function	oxygen evolving activity
A	0015979	biological_process	photosynthesis
A	0016168	molecular_function	chlorophyll binding
A	0016491	molecular_function	oxidoreductase activity
A	0016682	molecular_function	oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor
A	0019684	biological_process	photosynthesis, light reaction
A	0031676	cellular_component	plasma membrane-derived thylakoid membrane
A	0042651	cellular_component	thylakoid membrane
A	0046872	molecular_function	metal ion binding
B	0009521	cellular_component	photosystem
B	0009523	cellular_component	photosystem II
B	0009767	biological_process	photosynthetic electron transport chain
B	0009772	biological_process	photosynthetic electron transport in photosystem II
B	0015979	biological_process	photosynthesis
B	0016020	cellular_component	membrane
B	0016168	molecular_function	chlorophyll binding
B	0019684	biological_process	photosynthesis, light reaction
B	0031676	cellular_component	plasma membrane-derived thylakoid membrane
B	0042651	cellular_component	thylakoid membrane
C	0005737	cellular_component	cytoplasm
C	0009521	cellular_component	photosystem
C	0009523	cellular_component	photosystem II
C	0009767	biological_process	photosynthetic electron transport chain
C	0009772	biological_process	photosynthetic electron transport in photosystem II
C	0015979	biological_process	photosynthesis
C	0016020	cellular_component	membrane
C	0016168	molecular_function	chlorophyll binding
C	0019684	biological_process	photosynthesis, light reaction
C	0031676	cellular_component	plasma membrane-derived thylakoid membrane
C	0042651	cellular_component	thylakoid membrane
C	0046872	molecular_function	metal ion binding
D	0005506	molecular_function	iron ion binding
D	0005737	cellular_component	cytoplasm
D	0009055	molecular_function	electron transfer activity
D	0009523	cellular_component	photosystem II
D	0009772	biological_process	photosynthetic electron transport in photosystem II
D	0010242	molecular_function	oxygen evolving activity
D	0015979	biological_process	photosynthesis
D	0016020	cellular_component	membrane
D	0016168	molecular_function	chlorophyll binding
D	0016491	molecular_function	oxidoreductase activity
D	0019684	biological_process	photosynthesis, light reaction
D	0031676	cellular_component	plasma membrane-derived thylakoid membrane
D	0042651	cellular_component	thylakoid membrane
D	0046872	molecular_function	metal ion binding
E	0005506	molecular_function	iron ion binding
E	0005737	cellular_component	cytoplasm
E	0009055	molecular_function	electron transfer activity
E	0009523	cellular_component	photosystem II
E	0009539	cellular_component	photosystem II reaction center
E	0009767	biological_process	photosynthetic electron transport chain
E	0015979	biological_process	photosynthesis
E	0016020	cellular_component	membrane
E	0019684	biological_process	photosynthesis, light reaction
E	0020037	molecular_function	heme binding
E	0031676	cellular_component	plasma membrane-derived thylakoid membrane
E	0042651	cellular_component	thylakoid membrane
E	0046872	molecular_function	metal ion binding
F	0005506	molecular_function	iron ion binding
F	0005737	cellular_component	cytoplasm
F	0009055	molecular_function	electron transfer activity
F	0009523	cellular_component	photosystem II
F	0009539	cellular_component	photosystem II reaction center
F	0009767	biological_process	photosynthetic electron transport chain
F	0015979	biological_process	photosynthesis
F	0016020	cellular_component	membrane
F	0019684	biological_process	photosynthesis, light reaction
F	0020037	molecular_function	heme binding
F	0031676	cellular_component	plasma membrane-derived thylakoid membrane
F	0042651	cellular_component	thylakoid membrane
F	0046872	molecular_function	metal ion binding
H	0009523	cellular_component	photosystem II
H	0015979	biological_process	photosynthesis
H	0016020	cellular_component	membrane
H	0031676	cellular_component	plasma membrane-derived thylakoid membrane
H	0042301	molecular_function	phosphate ion binding
H	0042651	cellular_component	thylakoid membrane
H	0050821	biological_process	protein stabilization
I	0005737	cellular_component	cytoplasm
I	0009523	cellular_component	photosystem II
I	0009539	cellular_component	photosystem II reaction center
I	0015979	biological_process	photosynthesis
I	0016020	cellular_component	membrane
I	0031676	cellular_component	plasma membrane-derived thylakoid membrane
I	0042651	cellular_component	thylakoid membrane
J	0009523	cellular_component	photosystem II
J	0009539	cellular_component	photosystem II reaction center
J	0015979	biological_process	photosynthesis
J	0016020	cellular_component	membrane
J	0031676	cellular_component	plasma membrane-derived thylakoid membrane
J	0042651	cellular_component	thylakoid membrane
K	0005737	cellular_component	cytoplasm
K	0009523	cellular_component	photosystem II
K	0009539	cellular_component	photosystem II reaction center
K	0015979	biological_process	photosynthesis
K	0031676	cellular_component	plasma membrane-derived thylakoid membrane
K	0042651	cellular_component	thylakoid membrane
L	0005737	cellular_component	cytoplasm
L	0009523	cellular_component	photosystem II
L	0009539	cellular_component	photosystem II reaction center
L	0015979	biological_process	photosynthesis
L	0016020	cellular_component	membrane
L	0031676	cellular_component	plasma membrane-derived thylakoid membrane
L	0042651	cellular_component	thylakoid membrane
M	0005737	cellular_component	cytoplasm
M	0009523	cellular_component	photosystem II
M	0015979	biological_process	photosynthesis
M	0016020	cellular_component	membrane
M	0019684	biological_process	photosynthesis, light reaction
M	0031676	cellular_component	plasma membrane-derived thylakoid membrane
M	0042651	cellular_component	thylakoid membrane
O	0009654	cellular_component	photosystem II oxygen evolving complex
O	0010207	biological_process	photosystem II assembly
O	0010242	molecular_function	oxygen evolving activity
O	0042549	biological_process	photosystem II stabilization
R	0009523	cellular_component	photosystem II
R	0015979	biological_process	photosynthesis
R	0016020	cellular_component	membrane
R	0030145	molecular_function	manganese ion binding
R	0031676	cellular_component	plasma membrane-derived thylakoid membrane
R	0042651	cellular_component	thylakoid membrane
T	0009523	cellular_component	photosystem II
T	0009539	cellular_component	photosystem II reaction center
T	0015979	biological_process	photosynthesis
T	0016020	cellular_component	membrane
T	0031676	cellular_component	plasma membrane-derived thylakoid membrane
T	0042651	cellular_component	thylakoid membrane
U	0009523	cellular_component	photosystem II
U	0009654	cellular_component	photosystem II oxygen evolving complex
U	0015979	biological_process	photosynthesis
U	0019898	cellular_component	extrinsic component of membrane
U	0042549	biological_process	photosystem II stabilization
V	0005506	molecular_function	iron ion binding
V	0009055	molecular_function	electron transfer activity
V	0009523	cellular_component	photosystem II
V	0015979	biological_process	photosynthesis
V	0020037	molecular_function	heme binding
V	0022904	biological_process	respiratory electron transport chain
V	0042651	cellular_component	thylakoid membrane
X	0009523	cellular_component	photosystem II
X	0015979	biological_process	photosynthesis
X	0016020	cellular_component	membrane
X	0031676	cellular_component	plasma membrane-derived thylakoid membrane
X	0042651	cellular_component	thylakoid membrane
Y	0009523	cellular_component	photosystem II
Y	0015979	biological_process	photosynthesis
Y	0016020	cellular_component	membrane
Y	0031676	cellular_component	plasma membrane-derived thylakoid membrane
Y	0042651	cellular_component	thylakoid membrane
Z	0009523	cellular_component	photosystem II
Z	0009539	cellular_component	photosystem II reaction center
Z	0015979	biological_process	photosynthesis
Z	0031676	cellular_component	plasma membrane-derived thylakoid membrane
Z	0042549	biological_process	photosystem II stabilization
Z	0042651	cellular_component	thylakoid membrane
a	0005506	molecular_function	iron ion binding
a	0009055	molecular_function	electron transfer activity
a	0009523	cellular_component	photosystem II
a	0009635	biological_process	response to herbicide
a	0009772	biological_process	photosynthetic electron transport in photosystem II
a	0010242	molecular_function	oxygen evolving activity
a	0015979	biological_process	photosynthesis
a	0016168	molecular_function	chlorophyll binding
a	0016491	molecular_function	oxidoreductase activity
a	0016682	molecular_function	oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor
a	0019684	biological_process	photosynthesis, light reaction
a	0031676	cellular_component	plasma membrane-derived thylakoid membrane
a	0042651	cellular_component	thylakoid membrane
a	0046872	molecular_function	metal ion binding
b	0009521	cellular_component	photosystem
b	0009523	cellular_component	photosystem II
b	0009767	biological_process	photosynthetic electron transport chain
b	0009772	biological_process	photosynthetic electron transport in photosystem II
b	0015979	biological_process	photosynthesis
b	0016020	cellular_component	membrane
b	0016168	molecular_function	chlorophyll binding
b	0019684	biological_process	photosynthesis, light reaction
b	0031676	cellular_component	plasma membrane-derived thylakoid membrane
b	0042651	cellular_component	thylakoid membrane
c	0005737	cellular_component	cytoplasm
c	0009521	cellular_component	photosystem
c	0009523	cellular_component	photosystem II
c	0009767	biological_process	photosynthetic electron transport chain
c	0009772	biological_process	photosynthetic electron transport in photosystem II
c	0015979	biological_process	photosynthesis
c	0016020	cellular_component	membrane
c	0016168	molecular_function	chlorophyll binding
c	0019684	biological_process	photosynthesis, light reaction
c	0031676	cellular_component	plasma membrane-derived thylakoid membrane
c	0042651	cellular_component	thylakoid membrane
c	0046872	molecular_function	metal ion binding
d	0005506	molecular_function	iron ion binding
d	0005737	cellular_component	cytoplasm
d	0009055	molecular_function	electron transfer activity
d	0009523	cellular_component	photosystem II
d	0009772	biological_process	photosynthetic electron transport in photosystem II
d	0010242	molecular_function	oxygen evolving activity
d	0015979	biological_process	photosynthesis
d	0016020	cellular_component	membrane
d	0016168	molecular_function	chlorophyll binding
d	0016491	molecular_function	oxidoreductase activity
d	0019684	biological_process	photosynthesis, light reaction
d	0031676	cellular_component	plasma membrane-derived thylakoid membrane
d	0042651	cellular_component	thylakoid membrane
d	0046872	molecular_function	metal ion binding
e	0005506	molecular_function	iron ion binding
e	0005737	cellular_component	cytoplasm
e	0009055	molecular_function	electron transfer activity
e	0009523	cellular_component	photosystem II
e	0009539	cellular_component	photosystem II reaction center
e	0009767	biological_process	photosynthetic electron transport chain
e	0015979	biological_process	photosynthesis
e	0016020	cellular_component	membrane
e	0019684	biological_process	photosynthesis, light reaction
e	0020037	molecular_function	heme binding
e	0031676	cellular_component	plasma membrane-derived thylakoid membrane
e	0042651	cellular_component	thylakoid membrane
e	0046872	molecular_function	metal ion binding
f	0005506	molecular_function	iron ion binding
f	0005737	cellular_component	cytoplasm
f	0009055	molecular_function	electron transfer activity
f	0009523	cellular_component	photosystem II
f	0009539	cellular_component	photosystem II reaction center
f	0009767	biological_process	photosynthetic electron transport chain
f	0015979	biological_process	photosynthesis
f	0016020	cellular_component	membrane
f	0019684	biological_process	photosynthesis, light reaction
f	0020037	molecular_function	heme binding
f	0031676	cellular_component	plasma membrane-derived thylakoid membrane
f	0042651	cellular_component	thylakoid membrane
f	0046872	molecular_function	metal ion binding
h	0009523	cellular_component	photosystem II
h	0015979	biological_process	photosynthesis
h	0016020	cellular_component	membrane
h	0031676	cellular_component	plasma membrane-derived thylakoid membrane
h	0042301	molecular_function	phosphate ion binding
h	0042651	cellular_component	thylakoid membrane
h	0050821	biological_process	protein stabilization
i	0005737	cellular_component	cytoplasm
i	0009523	cellular_component	photosystem II
i	0009539	cellular_component	photosystem II reaction center
i	0015979	biological_process	photosynthesis
i	0016020	cellular_component	membrane
i	0031676	cellular_component	plasma membrane-derived thylakoid membrane
i	0042651	cellular_component	thylakoid membrane
j	0009523	cellular_component	photosystem II
j	0009539	cellular_component	photosystem II reaction center
j	0015979	biological_process	photosynthesis
j	0016020	cellular_component	membrane
j	0031676	cellular_component	plasma membrane-derived thylakoid membrane
j	0042651	cellular_component	thylakoid membrane
k	0005737	cellular_component	cytoplasm
k	0009523	cellular_component	photosystem II
k	0009539	cellular_component	photosystem II reaction center
k	0015979	biological_process	photosynthesis
k	0031676	cellular_component	plasma membrane-derived thylakoid membrane
k	0042651	cellular_component	thylakoid membrane
l	0005737	cellular_component	cytoplasm
l	0009523	cellular_component	photosystem II
l	0009539	cellular_component	photosystem II reaction center
l	0015979	biological_process	photosynthesis
l	0016020	cellular_component	membrane
l	0031676	cellular_component	plasma membrane-derived thylakoid membrane
l	0042651	cellular_component	thylakoid membrane
m	0005737	cellular_component	cytoplasm
m	0009523	cellular_component	photosystem II
m	0015979	biological_process	photosynthesis
m	0016020	cellular_component	membrane
m	0019684	biological_process	photosynthesis, light reaction
m	0031676	cellular_component	plasma membrane-derived thylakoid membrane
m	0042651	cellular_component	thylakoid membrane
o	0009654	cellular_component	photosystem II oxygen evolving complex
o	0010207	biological_process	photosystem II assembly
o	0010242	molecular_function	oxygen evolving activity
o	0042549	biological_process	photosystem II stabilization
r	0009523	cellular_component	photosystem II
r	0015979	biological_process	photosynthesis
r	0016020	cellular_component	membrane
r	0030145	molecular_function	manganese ion binding
r	0031676	cellular_component	plasma membrane-derived thylakoid membrane
r	0042651	cellular_component	thylakoid membrane
t	0009523	cellular_component	photosystem II
t	0009539	cellular_component	photosystem II reaction center
t	0015979	biological_process	photosynthesis
t	0016020	cellular_component	membrane
t	0031676	cellular_component	plasma membrane-derived thylakoid membrane
t	0042651	cellular_component	thylakoid membrane
u	0009523	cellular_component	photosystem II
u	0009654	cellular_component	photosystem II oxygen evolving complex
u	0015979	biological_process	photosynthesis
u	0019898	cellular_component	extrinsic component of membrane
u	0042549	biological_process	photosystem II stabilization
v	0005506	molecular_function	iron ion binding
v	0009055	molecular_function	electron transfer activity
v	0009523	cellular_component	photosystem II
v	0015979	biological_process	photosynthesis
v	0020037	molecular_function	heme binding
v	0022904	biological_process	respiratory electron transport chain
v	0042651	cellular_component	thylakoid membrane
x	0009523	cellular_component	photosystem II
x	0015979	biological_process	photosynthesis
x	0016020	cellular_component	membrane
x	0031676	cellular_component	plasma membrane-derived thylakoid membrane
x	0042651	cellular_component	thylakoid membrane
y	0009523	cellular_component	photosystem II
y	0015979	biological_process	photosynthesis
y	0016020	cellular_component	membrane
y	0031676	cellular_component	plasma membrane-derived thylakoid membrane
y	0042651	cellular_component	thylakoid membrane
z	0009523	cellular_component	photosystem II
z	0009539	cellular_component	photosystem II reaction center
z	0015979	biological_process	photosynthesis
z	0031676	cellular_component	plasma membrane-derived thylakoid membrane
z	0042549	biological_process	photosystem II stabilization
z	0042651	cellular_component	thylakoid membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue OEX A 601

Chain	Residue
A	ASP170
A	HOH709
C	GLU354
C	ARG357
A	GLU189
A	HIS332
A	GLU333
A	HIS337
A	ASP342
A	ALA344
A	HOH702
A	HOH706

site_id	AC2
Number of Residues	5
Details	binding site for residue FE2 A 602

Chain	Residue
A	HIS215
A	HIS272
A	BCT620
D	HIS214
D	HIS268

site_id	AC3
Number of Residues	15
Details	binding site for residue SQD A 603

Chain	Residue
A	LEU200
A	ASN267
A	SER270
A	PHE274
A	TRP278
A	GLY282
A	LHG617
A	HOH703
C	GLN28
C	TRP36
C	DGD517
D	PHE232
D	ARG233
K	ALA34
K	PHE37

site_id	AC4
Number of Residues	3
Details	binding site for residue CL A 604

Chain	Residue
A	HIS332
A	GLU333
D	LYS317

site_id	AC5
Number of Residues	3
Details	binding site for residue CL A 605

Chain	Residue
A	HIS337
A	ASN338
A	PHE339

site_id	AC6
Number of Residues	20
Details	binding site for residue CLA A 606

Chain	Residue
A	TYR147
A	PRO150
A	SER153
A	VAL157
A	MET183
A	PHE186
A	ILE192
A	LEU193
A	HIS198
A	GLY201
A	VAL202
A	PHE206
A	THR286
A	ALA287
A	ILE290
A	CLA607
A	PHO608
A	CLA615
D	CLA402
T	PHE17

site_id	AC7
Number of Residues	15
Details	binding site for residue CLA A 607

Chain	Residue
A	GLN199
A	VAL202
A	ALA203
A	GLY207
A	TRP278
A	CLA606
A	PL9611
A	HOH710
D	PHE157
D	VAL175
D	ILE178
D	PHE179
D	LEU182
D	PHO401
D	CLA402

site_id	AC8
Number of Residues	13
Details	binding site for residue PHO A 608

Chain	Residue
A	LEU41
A	THR45
A	TYR126
A	GLN130
A	TYR147
A	PRO279
A	VAL283
A	CLA606
A	CLA615
D	ALA208
D	LEU209
D	ILE213
D	TRP253

site_id	AC9
Number of Residues	16
Details	binding site for residue CLA A 609

Chain	Residue
I	THR13
I	PHE15
I	VAL16
A	ILE36
A	THR40
A	PHE93
A	TYR94
A	PRO95
A	ILE96
A	TRP97
A	LEU114
A	HIS118
A	LMG612
C	CLA505
C	CLA506
I	VAL12

site_id	AD1
Number of Residues	5
Details	binding site for residue BCR A 610

Chain	Residue
A	ILE38
A	LEU42
A	ALA43
A	SQD619
I	SQD101

site_id	AD2
Number of Residues	14
Details	binding site for residue PL9 A 611

Chain	Residue
A	PHE211
A	HIS215
A	LEU218
A	PHE255
A	ALA263
A	SER264
A	PHE265
A	LEU271
A	CLA607
D	LEU45
D	SQD409
F	ALA22
F	LEU26
X	THR24

site_id	AD3
Number of Residues	10
Details	binding site for residue LMG A 612

Chain	Residue
A	TRP97
A	GLU98
A	PHE117
A	CLA609
C	LEU214
C	PHE218
C	TRP223
C	CLA505
I	LYS5
I	TYR9

site_id	AD4
Number of Residues	9
Details	binding site for residue LMG A 613

Chain	Residue
A	ASN26
A	ARG27
A	LEU28
A	LEU42
A	CLA615
T	BCR101
b	TRP113
b	TYR117
b	BCR622

site_id	AD5
Number of Residues	17
Details	binding site for residue CLA A 615

Chain	Residue
A	PHE48
A	PHE158
A	MET172
A	ILE176
A	THR179
A	PHE180
A	MET183
A	CLA606
A	PHO608
A	LMG613
A	HOH705
D	MET198
D	VAL201
D	ALA202
D	GLY206
D	CLA402
D	PL9407

site_id	AD6
Number of Residues	12
Details	binding site for residue LHG A 616

Chain	Residue
A	SER232
A	ASN234
B	TYR6
B	ARG7
B	PHE464
B	TRP468
B	CLA611
D	TYR141
D	TRP266
D	PHE269
L	LHG101
M	PHE14

site_id	AD7
Number of Residues	17
Details	binding site for residue LHG A 617

Chain	Residue
A	ARG140
A	TRP142
A	PHE273
A	PHE285
A	SQD603
C	TRP443
C	ARG447
C	CLA504
C	CLA508
C	CLA510
C	DGD518
D	GLU219
D	ASN220
D	ALA229
D	SER230
D	THR231
D	PHE232

site_id	AD8
Number of Residues	8
Details	binding site for residue LHG A 618

Chain	Residue
A	LEU258
A	TYR262
A	SER264
A	PHE265
D	PHE27
E	PRO9
E	PHE10
E	SER11

site_id	AD9
Number of Residues	8
Details	binding site for residue SQD A 619

Chain	Residue
A	ASP103
A	LEU106
A	BCR610
I	SQD101
b	TRP75
b	GLY89
b	GLU94
b	LEU98

site_id	AE1
Number of Residues	9
Details	binding site for residue BCT A 620

Chain	Residue
A	HIS215
A	GLU244
A	TYR246
A	HIS272
A	FE2602
D	HIS214
D	TYR244
D	LYS264
D	HIS268

site_id	AE2
Number of Residues	8
Details	binding site for residue CLA B 601

Chain	Residue
B	TRP185
B	GLY186
B	PHE190
B	CLA602
B	LMG621
B	HOH710
H	PHE41
H	BCR102

site_id	AE3
Number of Residues	11
Details	binding site for residue CLA B 602

Chain	Residue
B	GLY189
B	GLY197
B	HIS201
B	PHE247
B	PHE250
B	CLA601
B	CLA603
D	LEU158
H	TYR49
H	BCR102
H	DGD103

site_id	AE4
Number of Residues	15
Details	binding site for residue CLA B 603

Chain	Residue
B	ARG68
B	LEU69
B	ALA146
B	CYS150
B	HIS201
B	HIS202
B	ALA248
B	VAL252
B	THR262
B	CLA602
B	CLA604
B	CLA605
B	CLA606
B	CLA609
H	PHE38

site_id	AE5
Number of Residues	15
Details	binding site for residue CLA B 604

Chain	Residue
B	TRP33
B	PHE61
B	PHE65
B	ARG68
B	VAL245
B	ALA248
B	ALA249
B	VAL252
B	PHE451
B	HIS455
B	PHE458
B	CLA603
B	CLA605
B	CLA607
B	CLA615

site_id	AE6
Number of Residues	17
Details	binding site for residue CLA B 605

Chain	Residue
B	THR27
B	VAL30
B	ALA31
B	TRP33
B	ALA34
B	VAL62
B	PHE65
B	MET66
B	ARG68
B	LEU69
B	VAL96
B	HIS100
B	LEU103
B	ALA205
B	CLA603
B	CLA604
B	CLA606

site_id	AE7
Number of Residues	15
Details	binding site for residue CLA B 606

Chain	Residue
B	LEU69
B	VAL71
B	PHE90
B	TRP91
B	VAL96
B	ALA99
B	HIS100
B	GLY152
B	PHE153
B	PHE156
B	HIS157
B	PHE162
B	PRO164
B	CLA603
B	CLA605

site_id	AE8
Number of Residues	12
Details	binding site for residue CLA B 607

Chain	Residue
B	TRP33
B	TYR40
B	GLY59
B	PHE61
B	THR327
B	GLY328
B	TRP450
B	ALA454
B	CLA604
B	LMG620
B	BCR627
B	HOH714

site_id	AE9
Number of Residues	13
Details	binding site for residue CLA B 608

Chain	Residue
B	THR236
B	SER239
B	ALA243
B	PHE246
B	PHE463
B	HIS466
B	CLA609
B	CLA610
D	PHE120
D	ILE123
D	MET126
D	CLA403
D	SQD408

site_id	AF1
Number of Residues	12
Details	binding site for residue CLA B 609

Chain	Residue
B	PHE139
B	ALA212
B	PHE215
B	HIS216
B	PRO221
B	PRO222
B	CLA603
B	CLA608
B	CLA610
H	THR27
H	MET31
H	BCR102

site_id	AF2
Number of Residues	12
Details	binding site for residue CLA B 610

Chain	Residue
B	LEU135
B	PHE139
B	HIS142
B	MET231
B	VAL237
B	SER240
B	SER241
B	CLA608
B	CLA609
B	CLA612
B	CLA615
B	HOH702

site_id	AF3
Number of Residues	17
Details	binding site for residue CLA B 611

Chain	Residue
A	LHG616
B	TRP5
B	TYR6
B	ARG7
B	VAL8
B	HIS9
B	THR10
B	ILE242
B	LEU461
B	PHE462
B	GLY465
B	TRP468
B	HIS469
B	ARG472
B	CLA612
B	CLA613
L	LHG101

site_id	AF4
Number of Residues	14
Details	binding site for residue CLA B 612

Chain	Residue
B	HIS9
B	LEU19
B	ALA22
B	HIS23
B	HIS26
B	THR27
B	VAL237
B	LEU238
B	SER241
B	CLA610
B	CLA611
B	CLA613
B	CLA614
B	CLA615

site_id	AF5
Number of Residues	8
Details	binding site for residue CLA B 613

Chain	Residue
B	HIS9
B	HIS26
B	VAL30
B	PHE462
B	CLA611
B	CLA612
B	CLA614
B	BCR617

site_id	AF6
Number of Residues	11
Details	binding site for residue CLA B 614

Chain	Residue
B	VAL8
B	HIS9
B	CLA612
B	CLA613
B	BCR617
B	LMG620
B	SQD626
L	GLN8
L	VAL10
M	PHE21
M	LEU25

site_id	AF7
Number of Residues	14
Details	binding site for residue CLA B 615

Chain	Residue
B	HIS23
B	LEU24
B	THR27
B	MET138
B	ILE141
B	HIS142
B	LEU145
B	CLA604
B	CLA610
B	CLA612
B	CLA616
H	LEU11
H	LEU14
H	ASN15

site_id	AF8
Number of Residues	8
Details	binding site for residue CLA B 616

Chain	Residue
B	ILE20
B	LEU24
B	ALA110
B	TRP113
B	HIS114
B	CLA615
B	BCR619
H	THR5

site_id	AF9
Number of Residues	10
Details	binding site for residue BCR B 617

Chain	Residue
B	MET25
B	LEU29
B	TRP115
B	CLA613
B	CLA614
B	BCR618
B	LMG620
B	SQD626
B	BCR627
M	LEU13

site_id	AG1
Number of Residues	9
Details	binding site for residue BCR B 618

Chain	Residue
B	LEU29
B	GLY32
B	SER36
B	VAL102
B	SER104
B	GLY105
B	BCR617
B	LMG625
B	BCR627

site_id	AG2
Number of Residues	6
Details	binding site for residue BCR B 619

Chain	Residue
B	LEU109
B	ALA110
B	CYS112
B	TRP113
B	CLA616
B	LMG625

site_id	AG3
Number of Residues	10
Details	binding site for residue LMG B 620

Chain	Residue
B	THR327
B	GLY328
B	PRO329
B	CLA607
B	CLA614
B	BCR617
L	LHG101
M	ASN4
M	GLN5
M	VAL17

site_id	AG4
Number of Residues	6
Details	binding site for residue LMG B 621

Chain	Residue
B	PRO183
B	GLU184
B	TRP185
B	CLA601
C	LEU204
H	PHE34

site_id	AG5
Number of Residues	7
Details	binding site for residue LMG B 625

Chain	Residue
B	TYR117
B	BCR618
B	BCR619
B	BCR627
a	LEU41
a	LEU42
a	THR45

site_id	AG6
Number of Residues	11
Details	binding site for residue SQD B 626

Chain	Residue
B	ARG18
B	TRP115
B	CLA614
B	BCR617
L	ARG7
l	ARG14
l	TYR18
t	CYS12
t	LEU16
t	PHE19
t	PHE23

site_id	AG7
Number of Residues	9
Details	binding site for residue BCR B 627

Chain	Residue
B	TRP33
B	SER36
B	MET37
B	CLA607
B	BCR617
B	BCR618
B	LMG625
t	PHE18
t	PHE22

site_id	AG8
Number of Residues	15
Details	binding site for residue CLA C 501

Chain	Residue
C	LEU95
C	LEU168
C	GLY171
C	ALA172
C	LEU175
C	HIS237
C	ILE240
C	MET282
C	PHE289
C	TYR297
C	CLA502
C	CLA503
C	CLA506
C	CLA507
C	BCR515

site_id	AG9
Number of Residues	15
Details	binding site for residue CLA C 502

Chain	Residue
C	TRP63
C	HIS91
C	LEU174
C	LYS178
C	LEU279
C	MET282
C	ALA286
C	TYR297
C	HIS430
C	LEU433
C	PHE437
C	CLA501
C	CLA503
C	CLA504
C	CLA510

site_id	AH1
Number of Residues	11
Details	binding site for residue CLA C 503

Chain	Residue
C	VAL61
C	THR68
C	LEU88
C	HIS91
C	ILE92
C	VAL114
C	HIS118
C	MET282
C	CLA501
C	CLA502
C	CLA510

site_id	AH2
Number of Residues	18
Details	binding site for residue CLA C 504

Chain	Residue
A	LHG617
C	TRP63
C	PHE70
C	GLN84
C	GLY85
C	ILE87
C	TRP425
C	SER429
C	HIS430
C	PHE436
C	CLA502
C	CLA508
C	DGD517
C	DGD518
C	LMG519
C	HOH601
K	PRO26
K	VAL30

site_id	AH3
Number of Residues	16
Details	binding site for residue CLA C 505

Chain	Residue
A	PHE33
A	LEU121
A	TRP131
A	CLA609
A	LMG612
C	PHE264
C	TYR274
C	GLY277
C	HIS441
C	LEU442
C	ALA445
C	ARG449
C	CLA507
C	BCR515
I	VAL16
I	PHE23

site_id	AH4
Number of Residues	15
Details	binding site for residue CLA C 506

Chain	Residue
A	CLA609
C	LEU161
C	LEU165
C	ILE243
C	GLY247
C	TRP250
C	HIS251
C	THR255
C	PHE257
C	TRP259
C	PHE264
C	CLA501
C	CLA507
C	BCR515
C	DGD516

site_id	AH5
Number of Residues	15
Details	binding site for residue CLA C 507

Chain	Residue
C	MET157
C	LEU161
C	HIS164
C	LEU168
C	PHE264
C	TRP266
C	TYR271
C	TYR274
C	SER275
C	LEU279
C	CLA501
C	CLA505
C	CLA506
C	CLA509
C	HOH603

site_id	AH6
Number of Residues	21
Details	binding site for residue CLA C 508

Chain	Residue
A	LHG617
C	PHE33
C	TRP36
C	ALA37
C	GLY38
C	ASN39
C	ALA40
C	LEU272
C	LEU276
C	PHE436
C	PHE437
C	GLY440
C	TRP443
C	HIS444
C	CLA504
C	CLA509
C	CLA510
C	CLA511
C	DGD517
C	LMG519
K	LEU33

site_id	AH7
Number of Residues	16
Details	binding site for residue CLA C 509

Chain	Residue
C	LEU49
C	ALA52
C	HIS53
C	HIS56
C	ILE160
C	HIS164
C	GLY268
C	TYR271
C	LEU272
C	SER275
C	LEU279
C	CLA507
C	CLA508
C	CLA510
C	CLA511
C	CLA512

site_id	AH8
Number of Residues	14
Details	binding site for residue CLA C 510

Chain	Residue
A	LHG617
C	ASN39
C	HIS56
C	LEU59
C	LEU279
C	PHE436
C	PHE437
C	CLA502
C	CLA503
C	CLA508
C	CLA509
C	CLA511
K	PRO29
K	LEU33

site_id	AH9
Number of Residues	19
Details	binding site for residue CLA C 511

Chain	Residue
C	ASN25
C	TRP35
C	GLY38
C	ASN39
C	ARG41
C	LEU42
C	LEU45
C	LYS48
C	HIS56
C	CLA508
C	CLA509
C	CLA510
K	PHE32
K	TRP39
K	GLN40
K	BCR101
Z	VAL20
Z	PRO24
Z	ALA28

site_id	AI1
Number of Residues	9
Details	binding site for residue CLA C 512

Chain	Residue
C	HIS53
C	ALA57
C	PHE147
C	PHE163
C	HIS164
C	VAL167
C	CLA509
C	CLA513
C	BCR514

site_id	AI2
Number of Residues	11
Details	binding site for residue CLA C 513

Chain	Residue
C	LEU50
C	VAL54
C	VAL124
C	GLY128
C	TYR131
C	HIS132
C	LEU140
C	TYR143
C	PHE147
C	CLA512
C	BCR514

site_id	AI3
Number of Residues	6
Details	binding site for residue BCR C 514

Chain	Residue
C	ILE120
C	SER121
C	VAL124
C	CLA512
C	CLA513
Z	GLY55

site_id	AI4
Number of Residues	10
Details	binding site for residue BCR C 515

Chain	Residue
C	ILE209
C	TYR212
C	LEU213
C	ASP232
C	GLY236
C	HIS237
C	PHE264
C	CLA501
C	CLA505
C	CLA506

site_id	AI5
Number of Residues	20
Details	binding site for residue DGD C 516

Chain	Residue
A	LEU91
A	PHE155
A	ILE163
C	PRO217
C	PHE218
C	GLY219
C	GLY220
C	GLU221
C	GLY222
C	TRP223
C	VAL227
C	CYS288
C	PHE292
C	ASN293
C	ASN294
C	THR295
C	ASP360
C	PHE361
C	ARG362
C	CLA506

site_id	AI6
Number of Residues	16
Details	binding site for residue DGD C 517

Chain	Residue
A	PHE197
A	SQD603
C	GLU83
C	GLN84
C	GLY85
C	LEU404
C	SER406
C	ASN418
C	PHE419
C	VAL420
C	TRP425
C	SER429
C	CLA504
C	CLA508
C	DGD518
C	LMG519

site_id	AI7
Number of Residues	21
Details	binding site for residue DGD C 518

Chain	Residue
A	PRO196
A	GLN199
A	ASN301
A	PHE302
A	SER305
A	LHG617
C	ASN405
C	SER406
C	VAL407
C	ASN415
C	SER416
C	ASN418
C	CLA504
C	DGD517
J	PHE29
J	ALA32
J	TYR33
J	GLY37
J	SER38
J	SER39
V	GLN34

site_id	AI8
Number of Residues	7
Details	binding site for residue LMG C 519

Chain	Residue
C	HIS74
C	CLA504
C	CLA508
C	DGD517
J	ILE22
K	VAL27
Y	GLN21

site_id	AI9
Number of Residues	6
Details	binding site for residue LMG C 520

Chain	Residue
B	ALA155
B	THR159
B	PRO183
C	LEU204
C	PRO206
C	HOH607

site_id	AJ1
Number of Residues	20
Details	binding site for residue PHO D 401

Chain	Residue
A	LEU210
A	MET214
A	LEU258
A	CLA607
D	ALA41
D	ALA44
D	TRP48
D	ILE114
D	GLY121
D	LEU122
D	PHE125
D	GLN129
D	ASN142
D	PHE146
D	PRO149
D	PHE153
D	GLY174
D	PRO275
D	LEU279
D	CLA402

site_id	AJ2
Number of Residues	20
Details	binding site for residue CLA D 402

Chain	Residue
A	MET183
A	CLA606
A	CLA607
A	CLA615
D	TRP48
D	PRO149
D	VAL152
D	VAL156
D	LEU182
D	PHE185
D	GLN186
D	TRP191
D	THR192
D	HIS197
D	GLY200
D	VAL201
D	VAL204
D	SER282
D	ALA283
D	PHO401

site_id	AJ3
Number of Residues	14
Details	binding site for residue CLA D 403

Chain	Residue
B	CLA608
D	ILE35
D	PRO39
D	LEU43
D	LEU89
D	LEU90
D	LEU91
D	LEU92
D	TRP93
D	THR112
D	PHE113
D	LEU116
D	HIS117
X	GLY13

site_id	AJ4
Number of Residues	10
Details	binding site for residue BCR D 404

Chain	Residue
D	TYR42
D	LEU43
D	GLY46
D	GLY47
D	LEU49
D	THR50
D	PHE101
D	LMG405
F	PRO29
F	PHE33

site_id	AJ5
Number of Residues	12
Details	binding site for residue LMG D 405

Chain	Residue
D	TYR67
D	CYS71
D	ASN72
D	PHE73
D	BCR404
F	THR30
F	MET40
F	GLN41
J	PHE28
J	GLY31
J	ALA32
J	LEU36

site_id	AJ6
Number of Residues	13
Details	binding site for residue LHG D 406

Chain	Residue
D	PHE257
D	ILE259
D	ALA260
D	PHE261
D	SER262
D	ASN263
D	TRP266
L	ASN13
L	THR15
L	LEU19
L	LHG101
T	PHE17
T	ALA20

site_id	AJ7
Number of Residues	17
Details	binding site for residue PL9 D 407

Chain	Residue
A	PHE52
A	ILE77
A	CLA615
D	MET199
D	LEU210
D	ILE213
D	HIS214
D	THR217
D	TRP253
D	ILE259
D	ALA260
D	PHE261
D	LEU267
D	VAL274
L	LEU23
L	LEU29
L	LHG101

site_id	AJ8
Number of Residues	9
Details	binding site for residue SQD D 408

Chain	Residue
B	ALA228
B	ARG230
B	LYS498
B	CLA608
D	ASP19
D	LYS23
D	TRP32
D	ARG134
D	LEU135

site_id	AJ9
Number of Residues	13
Details	binding site for residue SQD D 409

Chain	Residue
A	PL9611
D	ARG24
D	ARG26
E	GLU7
F	PHE16
F	THR17
F	VAL18
R	GLN30
R	LEU34
X	THR24
X	ILE31
X	ASP35
X	HOH101

site_id	AK1
Number of Residues	12
Details	binding site for residue HEM E 101

Chain	Residue
E	PHE10
E	ILE13
E	ARG18
E	TYR19
E	HIS23
E	LEU30
F	ILE15
F	ARG19
F	TRP20
F	HIS24
F	ALA27
F	ILE31

site_id	AK2
Number of Residues	5
Details	binding site for residue BCR H 102

Chain	Residue
B	CLA601
B	CLA602
B	CLA609
H	LEU37
H	PHE38

site_id	AK3
Number of Residues	15
Details	binding site for residue DGD H 103

Chain	Residue
B	TYR193
B	PHE250
B	TYR258
B	TYR273
B	GLN274
B	SER277
B	CLA602
D	HIS87
D	LEU162
H	LEU46
H	TYR49
H	ASN50
H	VAL60
H	SER61
H	TRP62

site_id	AK4
Number of Residues	7
Details	binding site for residue SQD I 101

Chain	Residue
A	LEU102
A	BCR610
A	SQD619
I	FME1
I	THR3
I	LEU4
I	PHE15

site_id	AK5
Number of Residues	6
Details	binding site for residue BCR K 101

Chain	Residue
C	LEU59
C	PHE62
C	ALA123
C	CLA511
K	PHE32
Z	SER16

site_id	AK6
Number of Residues	19
Details	binding site for residue LHG L 101

Chain	Residue
A	SER232
A	ASN234
A	LHG616
B	PRO4
B	TRP5
B	TYR6
B	CLA611
B	LMG620
D	TRP266
D	PHE273
D	LHG406
D	PL9407
L	GLU11
L	LEU12
L	ASN13
L	SER16
L	GLY20
L	LEU23
M	PHE21

site_id	AK7
Number of Residues	10
Details	binding site for residue BCR T 101

Chain	Residue
A	LMG613
T	PHE8
T	ALA15
T	PHE18
T	PHE22
b	TRP33
b	SER36
b	SQD601
b	CLA610
b	BCR621

site_id	AK8
Number of Residues	15
Details	binding site for residue HEC V 201

Chain	Residue
V	ALA36
V	CYS37
V	SER39
V	CYS40
V	HIS41
V	THR46
V	THR48
V	LEU52
V	ASP53
V	THR58
V	LEU59
V	TYR75
V	MET76
V	TYR82
V	HIS92

site_id	AK9
Number of Residues	13
Details	binding site for residue BCR Y 101

Chain	Residue
C	PHE62
J	THR15
K	LEU25
K	ILE28
K	LEU31
K	ALA34
K	VAL38
Y	ILE28
Y	GLY29
Y	GLY32
Z	VAL13
Z	SER16
Z	PHE17

site_id	AL1
Number of Residues	12
Details	binding site for residue OEX a 601

Chain	Residue
a	HOH701
a	HOH707
a	HOH711
c	GLU354
c	ARG357
a	ASP170
a	GLU189
a	HIS332
a	GLU333
a	HIS337
a	ASP342
a	ALA344

site_id	AL2
Number of Residues	5
Details	binding site for residue FE2 a 602

Chain	Residue
a	HIS215
a	HIS272
a	BCT605
d	HIS214
d	HIS268

site_id	AL3
Number of Residues	3
Details	binding site for residue CL a 603

Chain	Residue
a	HIS332
a	GLU333
d	LYS317

site_id	AL4
Number of Residues	2
Details	binding site for residue CL a 604

Chain	Residue
a	ASN338
a	PHE339

site_id	AL5
Number of Residues	8
Details	binding site for residue BCT a 605

Chain	Residue
a	HIS215
a	GLU244
a	TYR246
a	HIS272
a	FE2602
d	HIS214
d	TYR244
d	HIS268

site_id	AL6
Number of Residues	18
Details	binding site for residue CLA a 606

Chain	Residue
a	PRO150
a	SER153
a	VAL157
a	MET183
a	PHE186
a	ILE192
a	LEU193
a	HIS198
a	GLY201
a	VAL202
a	THR286
a	ILE290
a	CLA607
a	PHO608
a	CLA612
d	CLA403
d	LHG407
t	PHE17

site_id	AL7
Number of Residues	15
Details	binding site for residue CLA a 607

Chain	Residue
a	GLN199
a	VAL202
a	ALA203
a	PHE206
a	GLY207
a	TRP278
a	CLA606
a	HOH706
d	PHE157
d	VAL175
d	ILE178
d	PHE179
d	LEU182
d	PHO401
d	CLA403

site_id	AL8
Number of Residues	17
Details	binding site for residue PHO a 608

Chain	Residue
a	LEU41
a	ALA44
a	THR45
a	PHE48
a	TYR126
a	GLN130
a	ALA146
a	TYR147
a	PRO279
a	VAL283
a	CLA606
a	CLA612
d	ALA208
d	LEU209
d	ILE213
d	TRP253
d	PHE257

site_id	AL9
Number of Residues	14
Details	binding site for residue CLA a 609

Chain	Residue
a	PRO39
a	PHE93
a	TYR94
a	PRO95
a	ILE96
a	TRP97
a	LEU114
a	PHE117
a	HIS118
a	BCR610
c	CLA507
c	CLA508
i	TYR9
i	PHE15

site_id	AM1
Number of Residues	3
Details	binding site for residue BCR a 610

Chain	Residue
a	ALA43
a	ILE50
a	CLA609

site_id	AM2
Number of Residues	12
Details	binding site for residue PL9 a 611

Chain	Residue
a	HIS215
a	LEU218
a	ALA263
a	SER264
a	PHE265
a	LEU271
a	LEU275
a	LHG615
d	PHE38
d	PHO401
f	ALA22
x	THR24

site_id	AM3
Number of Residues	18
Details	binding site for residue CLA a 612

Chain	Residue
a	VAL157
a	PHE158
a	MET172
a	ILE176
a	THR179
a	PHE180
a	MET183
a	CLA606
a	PHO608
a	HOH710
d	MET198
d	VAL201
d	ALA202
d	GLY206
d	CLA403
d	LHG407
d	PL9408
l	LHG101

site_id	AM4
Number of Residues	13
Details	binding site for residue LHG a 613

Chain	Residue
a	SER232
a	ASN234
b	TYR6
b	ARG7
b	TRP468
b	CLA610
b	CLA614
d	TYR141
d	TRP266
d	PHE269
l	LHG101
m	PHE14
m	PRO18

site_id	AM5
Number of Residues	12
Details	binding site for residue LHG a 614

Chain	Residue
a	ARG140
a	TRP142
a	PHE273
c	TRP36
c	TRP443
c	ARG447
c	CLA510
d	GLU219
d	ASN220
d	ALA229
d	THR231
d	PHE232

site_id	AM6
Number of Residues	10
Details	binding site for residue LHG a 615

Chain	Residue
a	LEU258
a	PHE260
a	TYR262
a	ALA263
a	PL9611
d	PHE27
d	VAL28
e	PRO9
e	PHE10
e	SER11

site_id	AM7
Number of Residues	9
Details	binding site for residue SQD b 601

Chain	Residue
L	ARG14
L	TYR18
M	TYR26
T	CYS12
T	PHE23
T	BCR101
b	ARG18
b	CLA617
l	ARG7

site_id	AM8
Number of Residues	7
Details	binding site for residue CLA b 604

Chain	Residue
b	PHE190
b	CLA605
b	LMG624
b	HOH709
h	PHE41
h	LEU55
h	BCR101

site_id	AM9
Number of Residues	15
Details	binding site for residue CLA b 605

Chain	Residue
b	GLY189
b	PHE190
b	PRO192
b	GLY197
b	HIS201
b	ALA204
b	PHE247
b	PHE250
b	VAL251
b	CLA604
b	CLA606
d	LEU158
h	PHE41
h	ILE45
h	TYR49

site_id	AN1
Number of Residues	16
Details	binding site for residue CLA b 606

Chain	Residue
b	ARG68
b	LEU69
b	ALA146
b	CYS150
b	PHE153
b	HIS201
b	HIS202
b	ALA248
b	VAL252
b	THR262
b	CLA605
b	CLA607
b	CLA608
b	CLA609
b	CLA612
h	PHE38

site_id	AN2
Number of Residues	20
Details	binding site for residue CLA b 607

Chain	Residue
b	TRP33
b	PHE61
b	PHE65
b	ARG68
b	LEU145
b	LEU149
b	VAL245
b	ALA248
b	ALA249
b	VAL252
b	PHE451
b	HIS455
b	PHE458
b	CLA606
b	CLA608
b	CLA609
b	CLA610
b	CLA615
b	CLA616
b	CLA618

site_id	AN3
Number of Residues	19
Details	binding site for residue CLA b 608

Chain	Residue
b	THR27
b	VAL30
b	ALA31
b	TRP33
b	ALA34
b	VAL62
b	PHE65
b	MET66
b	ARG68
b	VAL96
b	HIS100
b	LEU103
b	LEU143
b	ALA205
b	CLA606
b	CLA607
b	CLA609
b	CLA612
b	CLA613

site_id	AN4
Number of Residues	17
Details	binding site for residue CLA b 609

Chain	Residue
b	LEU69
b	VAL71
b	PHE90
b	TRP91
b	VAL96
b	HIS100
b	LEU149
b	GLY152
b	PHE153
b	PHE156
b	HIS157
b	PHE162
b	PRO164
b	CLA606
b	CLA607
b	CLA608
b	BCR622

site_id	AN5
Number of Residues	12
Details	binding site for residue CLA b 610

Chain	Residue
T	BCR101
a	LHG613
b	TRP33
b	TYR40
b	GLY59
b	PHE61
b	THR327
b	GLY328
b	TRP450
b	CLA607
b	LMG623
b	HOH705

site_id	AN6
Number of Residues	16
Details	binding site for residue CLA b 611

Chain	Residue
b	THR236
b	SER239
b	ALA243
b	PHE247
b	PHE463
b	HIS466
b	ILE467
b	CLA612
b	CLA613
b	LMG625
d	PHE120
d	ILE123
d	MET126
d	CLA404
h	LEU43
h	DGD102

site_id	AN7
Number of Residues	15
Details	binding site for residue CLA b 612

Chain	Residue
b	PHE139
b	VAL208
b	ALA212
b	PHE215
b	HIS216
b	PRO221
b	PRO222
b	CLA606
b	CLA608
b	CLA611
b	CLA613
h	THR27
h	MET31
h	LEU42
h	BCR101

site_id	AN8
Number of Residues	14
Details	binding site for residue CLA b 613

Chain	Residue
b	LEU135
b	MET138
b	PHE139
b	HIS142
b	THR236
b	VAL237
b	SER240
b	SER241
b	CLA608
b	CLA611
b	CLA612
b	CLA615
b	CLA618
b	HOH707

site_id	AN9
Number of Residues	18
Details	binding site for residue CLA b 614

Chain	Residue
a	LHG613
b	TRP5
b	TYR6
b	ARG7
b	VAL8
b	HIS9
b	ILE242
b	PHE458
b	LEU461
b	PHE462
b	GLY465
b	TRP468
b	HIS469
b	ARG472
b	PHE479
b	CLA615
b	CLA616
l	LHG101

site_id	AO1
Number of Residues	17
Details	binding site for residue CLA b 615

Chain	Residue
b	HIS9
b	LEU12
b	LEU19
b	ALA22
b	HIS23
b	HIS26
b	THR27
b	VAL237
b	LEU238
b	SER241
b	VAL245
b	CLA607
b	CLA613
b	CLA614
b	CLA616
b	CLA617
b	CLA618

site_id	AO2
Number of Residues	10
Details	binding site for residue CLA b 616

Chain	Residue
b	HIS9
b	HIS26
b	VAL30
b	CLA607
b	CLA614
b	CLA615
b	CLA617
b	BCR620
b	LMG623
m	PHE14

site_id	AO3
Number of Residues	13
Details	binding site for residue CLA b 617

Chain	Residue
T	PHE8
b	VAL8
b	HIS9
b	VAL11
b	TRP115
b	SQD601
b	CLA615
b	CLA616
b	BCR620
b	LMG623
l	GLN8
l	VAL10
m	PHE21

site_id	AO4
Number of Residues	10
Details	binding site for residue CLA b 618

Chain	Residue
b	HIS23
b	MET138
b	HIS142
b	LEU145
b	CLA607
b	CLA613
b	CLA615
b	CLA619
h	LEU11
h	ASN15

site_id	AO5
Number of Residues	8
Details	binding site for residue CLA b 619

Chain	Residue
b	ILE20
b	LEU24
b	TRP113
b	HIS114
b	LEU120
b	CLA618
b	BCR622
h	THR5

site_id	AO6
Number of Residues	8
Details	binding site for residue BCR b 620

Chain	Residue
b	MET25
b	LEU29
b	TRP115
b	CLA616
b	CLA617
b	BCR621
b	LMG623
m	LEU13

site_id	AO7
Number of Residues	7
Details	binding site for residue BCR b 621

Chain	Residue
T	BCR101
b	LEU29
b	GLY32
b	SER36
b	VAL102
b	GLY105
b	BCR620

site_id	AO8
Number of Residues	6
Details	binding site for residue BCR b 622

Chain	Residue
A	LMG613
b	LEU109
b	CYS112
b	TRP113
b	CLA609
b	CLA619

site_id	AO9
Number of Residues	9
Details	binding site for residue LMG b 623

Chain	Residue
b	THR327
b	GLY328
b	PHE453
b	CLA610
b	CLA616
b	CLA617
b	BCR620
l	LHG101
m	ASN4

site_id	AP1
Number of Residues	4
Details	binding site for residue LMG b 624

Chain	Residue
b	GLU184
b	TRP185
b	CLA604
c	CLA514

site_id	AP2
Number of Residues	3
Details	binding site for residue LMG b 625

Chain	Residue
b	ALA228
b	CLA611
d	LMG409

site_id	AP3
Number of Residues	9
Details	binding site for residue SQD c 501

Chain	Residue
a	ASN267
a	SER270
a	PHE274
a	TRP278
c	GLN28
c	TRP36
d	PHE232
d	ARG233
k	PHE37

site_id	AP4
Number of Residues	12
Details	binding site for residue LMG c 502

Chain	Residue
a	TRP97
a	GLU98
c	LEU213
c	LEU214
c	LYS215
c	SER216
c	PHE218
c	TRP223
c	PHE284
c	CLA507
c	DGD518
i	TYR9

site_id	AP5
Number of Residues	15
Details	binding site for residue CLA c 503

Chain	Residue
c	LEU95
c	GLY171
c	ALA172
c	LEU175
c	VAL233
c	HIS237
c	MET282
c	PHE289
c	VAL296
c	TYR297
c	CLA504
c	CLA505
c	CLA508
c	CLA509
c	BCR517

site_id	AP6
Number of Residues	15
Details	binding site for residue CLA c 504

Chain	Residue
c	TRP63
c	HIS91
c	LEU174
c	PHE182
c	LEU279
c	MET282
c	ALA286
c	TYR297
c	HIS430
c	LEU433
c	PHE437
c	CLA503
c	CLA505
c	CLA506
c	CLA512

site_id	AP7
Number of Residues	12
Details	binding site for residue CLA c 505

Chain	Residue
c	ILE60
c	VAL61
c	THR68
c	LEU88
c	HIS91
c	ILE92
c	VAL114
c	HIS118
c	CLA503
c	CLA504
c	CLA512
c	CLA515

site_id	AP8
Number of Residues	17
Details	binding site for residue CLA c 506

Chain	Residue
c	TRP63
c	MET67
c	PHE70
c	GLN84
c	GLY85
c	ILE87
c	TRP425
c	SER429
c	HIS430
c	PHE436
c	CLA504
c	DGD519
c	DGD520
c	LMG521
c	HOH608
k	PRO26
k	VAL30

site_id	AP9
Number of Residues	15
Details	binding site for residue CLA c 507

Chain	Residue
a	PHE33
a	TRP131
a	CLA609
c	TYR274
c	GLY277
c	HIS441
c	LEU442
c	ALA445
c	ARG449
c	LMG502
c	CLA509
c	BCR517
i	VAL12
i	VAL16
i	PHE23

site_id	AQ1
Number of Residues	13
Details	binding site for residue CLA c 508

Chain	Residue
a	CLA609
c	LEU165
c	ILE243
c	GLY247
c	TRP250
c	HIS251
c	THR255
c	PHE257
c	TRP259
c	PHE264
c	CLA503
c	CLA509
c	BCR517

site_id	AQ2
Number of Residues	19
Details	binding site for residue CLA c 509

Chain	Residue
c	MET157
c	LEU161
c	HIS164
c	LEU168
c	TRP259
c	PHE264
c	TRP266
c	TYR271
c	TYR274
c	SER275
c	ALA278
c	LEU279
c	MET282
c	CLA503
c	CLA507
c	CLA508
c	CLA511
c	BCR517
c	HOH609

site_id	AQ3
Number of Residues	16
Details	binding site for residue CLA c 510

Chain	Residue
a	LHG614
c	PHE33
c	TRP36
c	ALA37
c	GLY38
c	ASN39
c	LEU272
c	LEU276
c	PHE436
c	PHE437
c	GLY440
c	TRP443
c	HIS444
c	CLA511
c	CLA512
c	CLA513

site_id	AQ4
Number of Residues	14
Details	binding site for residue CLA c 511

Chain	Residue
c	ASN39
c	LEU49
c	ALA52
c	HIS53
c	HIS56
c	GLY268
c	LEU272
c	SER275
c	LEU279
c	CLA509
c	CLA510
c	CLA512
c	CLA513
c	CLA514

site_id	AQ5
Number of Residues	11
Details	binding site for residue CLA c 512

Chain	Residue
c	ASN39
c	HIS56
c	LEU59
c	PHE437
c	CLA504
c	CLA505
c	CLA510
c	CLA511
c	CLA513
k	PRO29
k	LEU33

site_id	AQ6
Number of Residues	22
Details	binding site for residue CLA c 513

Chain	Residue
c	ASN25
c	ARG26
c	GLY38
c	ASN39
c	ARG41
c	LEU42
c	LEU45
c	LYS48
c	ILE134
c	CLA510
c	CLA511
c	CLA512
k	PHE32
k	LEU33
k	ALA36
k	TRP39
k	GLN40
k	BCR101
y	ASN45
y	LEU46
z	VAL20
z	ALA28

site_id	AQ7
Number of Residues	9
Details	binding site for residue CLA c 514

Chain	Residue
b	LMG624
c	HIS53
c	PHE147
c	PHE163
c	HIS164
c	ILE166
c	VAL167
c	CLA511
c	CLA515

site_id	AQ8
Number of Residues	13
Details	binding site for residue CLA c 515

Chain	Residue
c	LEU50
c	VAL54
c	VAL124
c	GLY128
c	TYR131
c	HIS132
c	PRO137
c	LEU140
c	TYR143
c	PHE147
c	CLA505
c	CLA514
c	BCR516

site_id	AQ9
Number of Residues	6
Details	binding site for residue BCR c 516

Chain	Residue
c	VAL116
c	SER121
c	CLA515
k	TYR15
z	GLY55
z	ASN58

site_id	AR1
Number of Residues	12
Details	binding site for residue BCR c 517

Chain	Residue
c	ILE209
c	LEU213
c	ASP232
c	GLY236
c	HIS237
c	ILE240
c	PHE264
c	CLA503
c	CLA507
c	CLA508
c	CLA509
i	LEU24

site_id	AR2
Number of Residues	17
Details	binding site for residue DGD c 518

Chain	Residue
a	PHE155
c	PRO217
c	GLY219
c	GLY220
c	GLU221
c	GLY222
c	VAL225
c	VAL227
c	CYS288
c	ASN293
c	ASN294
c	THR295
c	ASP360
c	PHE361
c	ARG362
c	LMG502
c	HOH610

site_id	AR3
Number of Residues	15
Details	binding site for residue DGD c 519

Chain	Residue
a	LEU297
c	GLU83
c	GLN84
c	GLY85
c	SER406
c	ASN418
c	PHE419
c	VAL420
c	TRP425
c	THR428
c	CLA506
c	DGD520
c	LMG521
j	PHE29
j	TYR33

site_id	AR4
Number of Residues	18
Details	binding site for residue DGD c 520

Chain	Residue
a	GLN199
a	PHE300
a	ASN301
a	SER305
c	ASN405
c	SER406
c	VAL407
c	ASN415
c	SER416
c	ASN418
c	CLA506
c	DGD519
j	PHE29
j	ALA32
j	TYR33
j	GLY37
j	SER38
v	GLN34

site_id	AR5
Number of Residues	7
Details	binding site for residue LMG c 521

Chain	Residue
c	HIS74
c	CLA506
c	DGD519
k	ASP23
k	VAL27
y	GLN21
y	ILE25

site_id	AR6
Number of Residues	8
Details	binding site for residue LMG c 522

Chain	Residue
b	PHE151
b	ALA155
b	THR159
b	PRO183
b	TRP185
b	ILE207
c	LEU204
c	PRO206

site_id	AR7
Number of Residues	20
Details	binding site for residue PHO d 401

Chain	Residue
a	ALA209
a	LEU210
a	MET214
a	LEU258
a	CLA607
a	PL9611
d	ALA41
d	ALA44
d	TRP48
d	GLY121
d	LEU122
d	PHE125
d	GLN129
d	ASN142
d	PHE146
d	PHE153
d	GLY174
d	PRO275
d	LEU279
d	CLA403

site_id	AR8
Number of Residues	19
Details	binding site for residue CLA d 403

Chain	Residue
a	PHE206
a	CLA606
a	CLA607
a	CLA612
d	PRO149
d	VAL152
d	VAL156
d	LEU182
d	PHE185
d	GLN186
d	TRP191
d	THR192
d	HIS197
d	GLY200
d	VAL201
d	VAL204
d	SER282
d	ALA283
d	PHO401

site_id	AR9
Number of Residues	16
Details	binding site for residue CLA d 404

Chain	Residue
b	CLA611
d	ILE35
d	PRO39
d	CYS40
d	LEU43
d	LEU89
d	LEU90
d	LEU91
d	LEU92
d	TRP93
d	THR112
d	PHE113
d	HIS117
h	LEU39
x	GLY13
x	LEU14

site_id	AS1
Number of Residues	9
Details	binding site for residue BCR d 405

Chain	Residue
d	TYR42
d	LEU43
d	GLY46
d	LEU49
d	LMG406
f	PRO29
f	THR30
f	PHE33
j	VAL21

site_id	AS2
Number of Residues	12
Details	binding site for residue LMG d 406

Chain	Residue
d	TYR67
d	CYS71
d	ASN72
d	PHE73
d	BCR405
f	THR30
f	MET40
f	GLN41
j	PHE28
j	GLY31
j	ALA32
j	LEU36

site_id	AS3
Number of Residues	15
Details	binding site for residue LHG d 407

Chain	Residue
a	CLA606
a	CLA612
d	PHE257
d	ILE259
d	ALA260
d	PHE261
d	SER262
d	ASN263
d	TRP266
d	PL9408
l	ASN13
l	THR15
l	LEU19
l	LHG101
t	PHE17

site_id	AS4
Number of Residues	17
Details	binding site for residue PL9 d 408

Chain	Residue
a	PHE52
a	CLA612
d	MET199
d	LEU210
d	ILE213
d	HIS214
d	THR217
d	TRP253
d	ALA260
d	PHE261
d	VAL274
d	LHG407
l	LEU23
l	VAL26
l	LEU27
l	LEU29
l	LHG101

site_id	AS5
Number of Residues	5
Details	binding site for residue LMG d 409

Chain	Residue
b	LMG625
d	ASP19
d	LYS23
d	TRP32
d	ARG134

site_id	AS6
Number of Residues	11
Details	binding site for residue HEM e 101

Chain	Residue
e	PHE10
e	ILE13
e	ARG18
e	TYR19
e	HIS23
e	LEU30
f	ILE15
f	ARG19
f	TRP20
f	HIS24
f	ILE31

site_id	AS7
Number of Residues	10
Details	binding site for residue SQD f 101

Chain	Residue
d	ARG24
d	ARG26
f	PHE16
f	THR17
f	VAL18
f	VAL21
r	GLN30
r	VAL31
r	LEU34
x	ASP35

site_id	AS8
Number of Residues	6
Details	binding site for residue BCR h 101

Chain	Residue
b	CLA604
b	CLA612
h	LEU37
h	PHE38
h	PHE41
h	ILE44

site_id	AS9
Number of Residues	13
Details	binding site for residue DGD h 102

Chain	Residue
b	PHE250
b	TYR258
b	TYR273
b	TYR279
b	CLA611
d	HIS87
d	LEU162
d	GLY163
h	TYR49
h	ASN50
h	VAL60
h	SER61
h	TRP62

site_id	AT1
Number of Residues	4
Details	binding site for residue BCR k 101

Chain	Residue
c	ALA123
c	CLA513
k	PHE32
z	SER16

site_id	AT2
Number of Residues	19
Details	binding site for residue LHG l 101

Chain	Residue
a	SER232
a	ASN234
a	CLA612
a	LHG613
b	PRO4
b	TRP5
b	TYR6
b	CLA614
b	LMG623
d	TRP266
d	PHE273
d	LHG407
d	PL9408
l	GLU11
l	LEU12
l	ASN13
l	SER16
l	GLY20
m	PHE21

site_id	AT3
Number of Residues	11
Details	binding site for residue BCR y 101

Chain	Residue
c	PHE62
j	THR15
k	ILE28
k	LEU31
k	ALA34
k	VAL38
y	ILE28
y	GLY29
y	GLY32
z	SER16
z	PHE17

site_id	AT4
Number of Residues	15
Details	binding site for Di-peptide HEM v 201 and CYS v 37

Chain	Residue
v	PHE33
v	TYR35
v	ALA36
v	ALA38
v	SER39
v	CYS40
v	HIS41
v	THR48
v	LEU52
v	ASP53
v	THR58
v	LEU59
v	TYR75
v	ILE88
v	HIS92

site_id	AT5
Number of Residues	17
Details	binding site for Di-peptide HEM v 201 and CYS v 40

Chain	Residue
v	ALA36
v	CYS37
v	ALA38
v	SER39
v	HIS41
v	VAL42
v	ILE45
v	THR46
v	LYS47
v	THR48
v	LEU52
v	ASP53
v	THR58
v	LEU59
v	TYR75
v	ILE88
v	HIS92

site_id	AT6
Number of Residues	15
Details	binding site for Di-peptide HEM v 201 and CYS v 37

Chain	Residue
v	PHE33
v	TYR35
v	ALA36
v	ALA38
v	SER39
v	CYS40
v	HIS41
v	THR48
v	LEU52
v	ASP53
v	THR58
v	LEU59
v	TYR75
v	ILE88
v	HIS92

Functional Information from PROSITE/UniProt

site_id	PS00244
Number of Residues	27
Details	REACTION_CENTER Photosynthetic reaction center proteins signature. NilmhPfHqlGvagvfggalfcAmHGS

Chain	Residue	Details
A	ASN191-SER217
D	ASN190-ALA216

site_id	PS00537
Number of Residues	15
Details	CYTOCHROME_B559 Cytochrome b559 subunits heme-binding site signature. IfTVRWvaVHTLAVP

Chain	Residue	Details
F	ILE15-PRO29
E	ILE14-PRO28

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	470
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	840
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	216
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Site: {"description":"Tyrosine radical intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11217865","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Site: {"description":"Stabilizes free radical intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	258
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	452
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	92
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01496","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	664
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	424
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	230
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_00642","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_00643","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"16172937","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	28
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	26
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	40
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00808","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"12881497","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgangb K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/b406989g"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI34
Number of Residues	6
Details	Topological domain: {"description":"Lumenal"}

Chain

Residue

Details

site_id	SWS_FT_FI35
Number of Residues	2
Details	Modified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI36
Number of Residues	36
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00717","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)