Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6DHH

RT XFEL structure of Photosystem II 400 microseconds after the second illumination at 2.2 Angstrom resolution

This is a non-PDB format compatible entry.

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	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
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	0009523	cellular_component	photosystem II
K	0009539	cellular_component	photosystem II reaction center
K	0015979	biological_process	photosynthesis
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	0009523	cellular_component	photosystem II
O	0009654	cellular_component	photosystem II oxygen evolving complex
O	0010207	biological_process	photosystem II assembly
O	0010242	molecular_function	oxygen evolving activity
O	0015979	biological_process	photosynthesis
O	0031676	cellular_component	plasma membrane-derived thylakoid membrane
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
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	0031676	cellular_component	plasma membrane-derived thylakoid membrane
U	0042549	biological_process	photosystem II stabilization
U	0042651	cellular_component	thylakoid membrane
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	0019684	biological_process	photosynthesis, light reaction
V	0020037	molecular_function	heme binding
V	0022904	biological_process	respiratory electron transport chain
V	0031676	cellular_component	plasma membrane-derived thylakoid membrane
V	0042651	cellular_component	thylakoid membrane
V	0046872	molecular_function	metal ion binding
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
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	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
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	0009523	cellular_component	photosystem II
k	0009539	cellular_component	photosystem II reaction center
k	0015979	biological_process	photosynthesis
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	0009523	cellular_component	photosystem II
o	0009654	cellular_component	photosystem II oxygen evolving complex
o	0010207	biological_process	photosystem II assembly
o	0010242	molecular_function	oxygen evolving activity
o	0015979	biological_process	photosynthesis
o	0031676	cellular_component	plasma membrane-derived thylakoid membrane
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
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	0031676	cellular_component	plasma membrane-derived thylakoid membrane
u	0042549	biological_process	photosystem II stabilization
u	0042651	cellular_component	thylakoid membrane
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	0019684	biological_process	photosynthesis, light reaction
v	0020037	molecular_function	heme binding
v	0022904	biological_process	respiratory electron transport chain
v	0031676	cellular_component	plasma membrane-derived thylakoid membrane
v	0042651	cellular_component	thylakoid membrane
v	0046872	molecular_function	metal ion binding
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
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	5
Details	binding site for residue FE2 A 401

Chain	Residue
A	HIS215
A	HIS272
A	BCT415
D	HIS214
D	HIS268

site_id	AC2
Number of Residues	3
Details	binding site for residue CL A 402

Chain	Residue
A	ASN181
A	GLU333
D	LYS317

site_id	AC3
Number of Residues	2
Details	binding site for residue CL A 403

Chain	Residue
C	GLU354
A	ASN338

site_id	AC4
Number of Residues	19
Details	binding site for residue CLA A 404

Chain	Residue
A	TYR147
A	SER153
A	VAL157
A	MET183
A	PHE186
A	GLN187
A	ILE192
A	HIS198
A	GLY201
A	PHE206
A	THR286
A	ALA287
A	ILE290
A	CLA405
A	PHO406
D	LEU205
D	CLA402
D	CLA403
T	PHE17

site_id	AC5
Number of Residues	17
Details	binding site for residue CLA A 405

Chain	Residue
A	GLN199
A	VAL202
A	ALA203
A	LEU210
A	TRP278
A	CLA404
A	HOH549
A	HOH603
C	DGD518
D	VAL175
D	ILE178
D	PHE179
D	LEU182
D	PHO401
D	CLA403
D	LMG407
D	HOH612

site_id	AC6
Number of Residues	13
Details	binding site for residue PHO A 406

Chain	Residue
A	LEU41
A	ALA44
A	THR45
A	PHE48
A	TYR126
A	GLN130
A	TYR147
A	PRO279
A	CLA404
D	LEU209
D	ILE213
D	TRP253
D	CLA402

site_id	AC7
Number of Residues	14
Details	binding site for residue CLA A 407

Chain	Residue
A	ILE36
A	THR40
A	PHE93
A	PRO95
A	ILE96
A	TRP97
A	LEU114
A	PHE117
A	HIS118
A	LMG410
I	VAL11
I	VAL12
I	THR13
I	PHE15

site_id	AC8
Number of Residues	1
Details	binding site for residue BCR A 408

Chain	Residue
A	ILE50

site_id	AC9
Number of Residues	13
Details	binding site for residue PL9 A 409

Chain	Residue
A	MET214
A	HIS215
A	LEU218
A	PHE255
A	SER264
A	PHE265
A	LEU271
D	TYR42
D	PHO401
D	CLA403
E	LHG101
F	ALA22
F	SQD101

site_id	AD1
Number of Residues	14
Details	binding site for residue LMG A 410

Chain	Residue
I	LYS5
I	TYR9
A	TRP97
A	GLU98
A	SER124
A	PHE155
A	CLA407
C	LEU214
C	LYS215
C	SER216
C	GLU221
C	TRP223
C	CLA505
C	HOH680

site_id	AD2
Number of Residues	13
Details	binding site for residue SQD A 411

Chain	Residue
A	LEU200
A	ASN267
A	SER270
A	TRP278
A	VAL281
A	GLY282
C	TRP36
C	CLA508
C	HOH685
D	SER230
D	PHE232
D	ARG233
K	PHE37

site_id	AD3
Number of Residues	10
Details	binding site for residue SQD A 412

Chain	Residue
A	ARG27
A	LEU28
A	HOH635
D	LHG408
T	PHE22
T	BCR101
b	LEU106
b	CLA607
b	CLA617
b	BCR620

site_id	AD4
Number of Residues	13
Details	binding site for residue DGD A 413

Chain	Residue
A	LEU42
A	ILE50
A	LEU102
A	ASP103
A	HOH501
A	HOH537
A	HOH609
O	LYS69
O	GLN109
O	GLY113
b	TRP75
b	SER76
b	CLA607

site_id	AD5
Number of Residues	17
Details	binding site for residue OEY A 414

Chain	Residue
A	ASP61
A	ASP170
A	VAL185
A	GLU189
A	HIS332
A	GLU333
A	HIS337
A	ASP342
A	ALA344
A	HOH504
A	HOH508
A	HOH515
A	HOH523
A	HOH575
A	HOH577
C	GLU354
C	ARG357

site_id	AD6
Number of Residues	9
Details	binding site for residue BCT A 415

Chain	Residue
A	HIS215
A	GLU244
A	TYR246
A	HIS272
A	FE2401
D	HIS214
D	TYR244
D	LYS264
D	HIS268

site_id	AD7
Number of Residues	6
Details	binding site for residue CLA B 601

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

site_id	AD8
Number of Residues	15
Details	binding site for residue CLA B 602

Chain	Residue
B	GLY189
B	PHE190
B	PRO192
B	GLY197
B	ALA200
B	HIS201
B	ALA205
B	VAL208
B	PHE247
B	PHE250
B	CLA601
B	CLA603
D	ILE159
H	ILE45
H	DGD102

site_id	AD9
Number of Residues	17
Details	binding site for residue CLA B 603

Chain	Residue
B	ARG68
B	LEU69
B	ALA146
B	CYS150
B	PHE153
B	MET166
B	HIS201
B	HIS202
B	VAL252
B	THR262
B	CLA602
B	CLA604
B	CLA605
B	CLA606
B	HOH748
H	PHE38
H	BCR101

site_id	AE1
Number of Residues	17
Details	binding site for residue CLA B 604

Chain	Residue
B	TRP33
B	PHE61
B	PHE65
B	ARG68
B	LEU149
B	VAL245
B	ALA248
B	ALA249
B	VAL252
B	PHE451
B	HIS455
B	PHE458
B	CLA603
B	CLA605
B	CLA607
B	CLA612
B	CLA613

site_id	AE2
Number of Residues	17
Details	binding site for residue CLA B 605

Chain	Residue
B	THR27
B	VAL30
B	ALA31
B	ALA34
B	VAL62
B	MET66
B	ARG68
B	LEU69
B	VAL96
B	HIS100
B	ALA205
B	GLY209
B	CLA603
B	CLA604
B	CLA606
B	CLA610
B	HOH730

site_id	AE3
Number of Residues	17
Details	binding site for residue CLA B 606

Chain	Residue
B	LEU69
B	TRP91
B	VAL96
B	ALA99
B	VAL102
B	LEU149
B	GLY152
B	PHE153
B	PHE156
B	HIS157
B	PHE162
B	GLY163
B	PRO164
B	CLA603
B	CLA605
B	BCR619
a	SQD412

site_id	AE4
Number of Residues	17
Details	binding site for residue CLA B 607

Chain	Residue
B	TRP33
B	TYR40
B	GLN58
B	GLY59
B	PHE61
B	LEU324
B	THR327
B	GLY328
B	PRO329
B	TRP450
B	ALA454
B	CLA604
B	CLA613
B	LMG620
B	LHG622
B	HOH873
D	MET281

site_id	AE5
Number of Residues	13
Details	binding site for residue CLA B 608

Chain	Residue
B	THR236
B	SER239
B	SER240
B	ALA243
B	PHE463
B	HIS466
B	CLA609
B	CLA610
B	HOH792
D	MET126
D	LEU127
D	LMG411
H	LEU43

site_id	AE6
Number of Residues	14
Details	binding site for residue CLA B 609

Chain	Residue
B	PHE139
B	VAL208
B	ALA212
B	PHE215
B	HIS216
B	VAL219
B	PRO221
B	PRO222
B	CLA608
B	CLA610
D	LMG411
H	THR27
H	MET31
H	BCR101

site_id	AE7
Number of Residues	12
Details	binding site for residue CLA B 610

Chain	Residue
B	PHE139
B	HIS142
B	THR236
B	VAL237
B	SER240
B	SER241
B	CLA605
B	CLA608
B	CLA609
B	CLA612
B	CLA615
B	HOH772

site_id	AE8
Number of Residues	16
Details	binding site for residue CLA B 611

Chain	Residue
B	TRP5
B	TYR6
B	ARG7
B	VAL8
B	HIS9
B	LEU238
B	LEU461
B	PHE462
B	GLY465
B	TRP468
B	HIS469
B	ARG472
B	CLA612
B	CLA613
B	BCR618
B	HOH803

site_id	AE9
Number of Residues	16
Details	binding site for residue CLA B 612

Chain	Residue
B	HIS9
B	LEU19
B	HIS23
B	HIS26
B	THR27
B	ILE234
B	VAL237
B	LEU238
B	SER241
B	CLA604
B	CLA610
B	CLA611
B	CLA613
B	CLA614
B	CLA615
B	HOH799

site_id	AF1
Number of Residues	12
Details	binding site for residue CLA B 613

Chain	Residue
B	HIS9
B	HIS26
B	TRP33
B	PHE462
B	CLA604
B	CLA607
B	CLA611
B	CLA612
B	CLA614
B	BCR617
B	LMG620
B	LHG622

site_id	AF2
Number of Residues	10
Details	binding site for residue CLA B 614

Chain	Residue
B	VAL8
B	HIS9
B	LEU12
B	CLA612
B	CLA613
B	BCR617
B	SQD623
L	VAL10
L	LHG101
M	PHE21

site_id	AF3
Number of Residues	10
Details	binding site for residue CLA B 615

Chain	Residue
B	ILE20
B	HIS23
B	MET138
B	HIS142
B	LEU145
B	CLA610
B	CLA612
B	CLA616
H	LEU11
H	LEU14

site_id	AF4
Number of Residues	10
Details	binding site for residue CLA B 616

Chain	Residue
B	LEU24
B	TRP113
B	HIS114
B	CLA615
B	BCR619
B	HOH836
B	HOH856
H	THR5
H	GLY8
a	SQD412

site_id	AF5
Number of Residues	5
Details	binding site for residue BCR B 617

Chain	Residue
B	MET25
B	CLA613
B	CLA614
B	BCR618
B	SQD623

site_id	AF6
Number of Residues	11
Details	binding site for residue BCR B 618

Chain	Residue
B	LEU29
B	GLY32
B	TRP33
B	SER36
B	ILE101
B	VAL102
B	SER104
B	GLY105
B	CLA611
B	BCR617
t	BCR101

site_id	AF7
Number of Residues	6
Details	binding site for residue BCR B 619

Chain	Residue
B	LEU106
B	LEU107
B	LEU109
B	CLA606
B	CLA616
a	SQD412

site_id	AF8
Number of Residues	12
Details	binding site for residue LMG B 620

Chain	Residue
B	THR327
B	GLY328
B	PRO329
B	LYS332
B	PHE453
B	CLA607
B	CLA613
L	PHE35
L	LHG101
M	ASN4
M	LEU6
M	ALA10

site_id	AF9
Number of Residues	17
Details	binding site for residue LHG B 622

Chain	Residue
A	SER232
A	ALA233
A	ASN234
B	TYR6
B	ARG7
B	LEU461
B	TRP468
B	CLA607
B	CLA613
B	HOH803
D	TYR141
D	PHE269
D	THR277
D	HOH561
L	LHG101
M	PHE14
M	PRO18

site_id	AG1
Number of Residues	12
Details	binding site for residue SQD B 623

Chain	Residue
B	ARG18
B	TRP115
B	CLA614
B	BCR617
B	HOH766
B	HOH773
B	HOH812
B	HOH852
L	ARG7
l	ARG14
l	TYR18
t	PHE23

site_id	AG2
Number of Residues	17
Details	binding site for residue CLA C 501

Chain	Residue
C	THR94
C	LEU95
C	LEU168
C	GLY171
C	ALA172
C	VAL233
C	HIS237
C	ALA278
C	MET282
C	PHE289
C	TYR297
C	CLA502
C	CLA503
C	CLA506
C	CLA507
C	BCR515
C	HOH662

site_id	AG3
Number of Residues	16
Details	binding site for residue CLA C 502

Chain	Residue
C	TRP63
C	HIS91
C	LEU95
C	LEU174
C	LEU279
C	MET282
C	ALA286
C	TYR297
C	LEU426
C	HIS430
C	LEU433
C	PHE437
C	CLA501
C	CLA503
C	CLA510
C	CLA512

site_id	AG4
Number of Residues	13
Details	binding site for residue CLA C 503

Chain	Residue
C	ILE60
C	THR68
C	LEU88
C	HIS91
C	VAL114
C	HIS118
C	LEU279
C	CLA501
C	CLA502
C	CLA507
C	CLA512
C	CLA513
C	HOH662

site_id	AG5
Number of Residues	14
Details	binding site for residue CLA C 504

Chain	Residue
C	TRP63
C	MET67
C	PHE70
C	GLN84
C	GLY85
C	TRP425
C	SER429
C	CLA508
C	DGD517
C	LMG519
C	HOH647
C	HOH752
D	LHG409
K	PRO26

site_id	AG6
Number of Residues	15
Details	binding site for residue CLA C 505

Chain	Residue
A	PHE33
A	TRP131
A	LMG410
C	PHE264
C	TYR274
C	GLY277
C	ALA278
C	HIS441
C	LEU442
C	ALA445
C	ARG449
C	CLA507
C	BCR515
C	HOH658
I	PHE23

site_id	AG7
Number of Residues	15
Details	binding site for residue CLA C 506

Chain	Residue
C	LEU161
C	LEU213
C	ILE243
C	GLY247
C	TRP250
C	HIS251
C	THR254
C	THR255
C	PRO256
C	PHE257
C	TRP259
C	CLA501
C	CLA507
C	BCR515
C	DGD516

site_id	AG8
Number of Residues	16
Details	binding site for residue CLA C 507

Chain	Residue
C	MET157
C	LEU161
C	HIS164
C	LEU168
C	ILE240
C	TYR271
C	TYR274
C	SER275
C	ALA278
C	MET282
C	CLA501
C	CLA503
C	CLA505
C	CLA506
C	CLA509
C	HOH637

site_id	AG9
Number of Residues	17
Details	binding site for residue CLA C 508

Chain	Residue
A	SQD411
C	TRP36
C	ALA37
C	GLY38
C	ASN39
C	ALA40
C	LEU276
C	PHE436
C	GLY440
C	TRP443
C	HIS444
C	ARG447
C	CLA504
C	CLA509
C	CLA510
C	HOH727
D	LHG409

site_id	AH1
Number of Residues	18
Details	binding site for residue CLA C 509

Chain	Residue
C	ASN39
C	LEU49
C	ALA52
C	HIS53
C	HIS56
C	TYR149
C	TRP151
C	GLY268
C	GLU269
C	TYR271
C	LEU272
C	SER275
C	LEU279
C	CLA507
C	CLA508
C	CLA510
C	CLA511
C	CLA512

site_id	AH2
Number of Residues	11
Details	binding site for residue CLA C 510

Chain	Residue
C	ASN39
C	HIS56
C	LEU59
C	PHE436
C	PHE437
C	CLA502
C	CLA508
C	CLA509
C	CLA511
K	PRO29
K	LEU33

site_id	AH3
Number of Residues	21
Details	binding site for residue CLA C 511

Chain	Residue
C	TRP35
C	GLY38
C	ASN39
C	ARG41
C	LEU42
C	LYS48
C	GLY126
C	PHE127
C	ILE134
C	CLA509
C	CLA510
C	BCR520
K	PHE32
K	LEU33
K	TRP39
K	GLN40
K	ARG46
Y	LEU39
Y	ASN45
Y	LEU46
Z	VAL20

site_id	AH4
Number of Residues	14
Details	binding site for residue CLA C 512

Chain	Residue
C	LEU50
C	HIS53
C	PHE146
C	PHE147
C	PHE163
C	HIS164
C	VAL167
C	ILE170
C	GLY171
C	CLA502
C	CLA503
C	CLA509
C	CLA513
C	HOH684

site_id	AH5
Number of Residues	11
Details	binding site for residue CLA C 513

Chain	Residue
C	LEU50
C	VAL124
C	GLY128
C	TYR131
C	HIS132
C	PRO137
C	TYR143
C	PHE147
C	CLA503
C	CLA512
C	BCR514

site_id	AH6
Number of Residues	6
Details	binding site for residue BCR C 514

Chain	Residue
C	SER121
C	CLA513
K	TYR15
Z	VAL54
Z	GLY55
Z	ASN58

site_id	AH7
Number of Residues	9
Details	binding site for residue BCR C 515

Chain	Residue
C	ILE209
C	LEU213
C	GLY236
C	HIS237
C	PHE264
C	CLA501
C	CLA505
C	CLA506
I	LEU24

site_id	AH8
Number of Residues	23
Details	binding site for residue DGD C 516

Chain	Residue
A	LEU91
A	LEU151
A	PHE155
C	PRO217
C	GLY219
C	GLY220
C	GLU221
C	GLY222
C	TRP223
C	VAL225
C	VAL227
C	PHE284
C	ASN293
C	ASN294
C	THR295
C	ASP360
C	PHE361
C	ARG362
C	CLA506
C	HOH638
C	HOH690
C	HOH699
C	HOH720

site_id	AH9
Number of Residues	16
Details	binding site for residue DGD C 517

Chain	Residue
A	HIS195
A	PHE197
C	GLU83
C	GLN84
C	GLY85
C	SER406
C	ASN418
C	PHE419
C	VAL420
C	TRP425
C	THR428
C	CLA504
C	DGD518
C	LMG519
C	HOH622
J	HOH210

site_id	AI1
Number of Residues	19
Details	binding site for residue DGD C 518

Chain	Residue
A	PRO196
A	LEU200
A	PHE285
A	ASN301
A	SER305
A	CLA405
C	ASN405
C	ASN415
C	SER416
C	ASN418
C	DGD517
C	HOH682
J	PHE29
J	ALA32
J	TYR33
J	GLY37
J	SER38
J	SER39
V	GLN34

site_id	AI2
Number of Residues	8
Details	binding site for residue LMG C 519

Chain	Residue
C	HIS74
C	CLA504
C	DGD517
C	HOH605
C	HOH698
K	ASP23
K	LEU31
Y	GLN21

site_id	AI3
Number of Residues	10
Details	binding site for residue BCR C 520

Chain	Residue
C	GLY58
C	LEU119
C	SER122
C	ALA123
C	GLY126
C	CLA511
K	PHE32
K	TRP39
K	BCR101
Z	SER16

site_id	AI4
Number of Residues	16
Details	binding site for residue PHO D 401

Chain	Residue
A	PHE206
A	ALA209
A	LEU210
A	MET214
A	CLA405
A	PL9409
D	TRP48
D	ILE114
D	GLY121
D	LEU122
D	PHE125
D	GLN129
D	ASN142
D	GLY174
D	PRO275
D	CLA403

site_id	AI5
Number of Residues	13
Details	binding site for residue CLA D 402

Chain	Residue
A	MET172
A	ILE176
A	THR179
A	MET183
A	CLA404
A	PHO406
D	MET198
D	VAL201
D	ALA202
D	PL9406
D	HOH533
D	HOH575
D	HOH605

site_id	AI6
Number of Residues	17
Details	binding site for residue CLA D 403

Chain	Residue
A	CLA404
A	CLA405
A	PL9409
D	VAL152
D	SER155
D	VAL156
D	LEU182
D	PHE185
D	TRP191
D	THR192
D	HIS197
D	GLY200
D	VAL204
D	SER282
D	ALA283
D	VAL286
D	PHO401

site_id	AI7
Number of Residues	17
Details	binding site for residue CLA D 404

Chain	Residue
D	CYS40
D	LEU43
D	LEU89
D	LEU90
D	LEU91
D	LEU92
D	TRP93
D	TRP104
D	THR112
D	PHE113
D	LEU116
D	HIS117
H	HOH205
X	GLY13
X	LEU14
X	ALA18
X	VAL20

site_id	AI8
Number of Residues	7
Details	binding site for residue BCR D 405

Chain	Residue
D	TYR42
D	GLY46
D	LEU49
D	THR50
D	LMG407
F	PHE33
F	LEU34

site_id	AI9
Number of Residues	16
Details	binding site for residue PL9 D 406

Chain	Residue
A	PHE52
A	ILE53
D	MET198
D	MET199
D	HIS214
D	THR217
D	MET246
D	TRP253
D	ALA260
D	PHE261
D	LEU267
D	PHE270
D	CLA402
L	LEU29
L	LHG101
T	PHE10

site_id	AJ1
Number of Residues	18
Details	binding site for residue LMG D 407

Chain	Residue
A	CLA405
C	HOH682
D	TYR67
D	CYS71
D	ASN72
D	PHE73
D	BCR405
E	LHG101
F	LEU26
F	THR30
F	ILE37
F	MET40
F	GLN41
J	PHE28
J	GLY31
J	ALA32
J	LEU36
J	HOH201

site_id	AJ2
Number of Residues	13
Details	binding site for residue LHG D 408

Chain	Residue
A	SQD412
D	ILE256
D	ALA260
D	PHE261
D	SER262
D	ASN263
D	TRP266
D	HOH502
D	HOH516
D	HOH543
L	THR15
L	LHG101
T	PHE17

site_id	AJ3
Number of Residues	14
Details	binding site for residue LHG D 409

Chain	Residue
A	ARG140
A	TRP142
A	PHE273
C	TRP36
C	TRP443
C	ARG447
C	CLA504
C	CLA508
D	GLU219
D	ASN220
D	ALA229
D	THR231
D	PHE232
D	HOH529

site_id	AJ4
Number of Residues	5
Details	binding site for residue LMG D 410

Chain	Residue
B	ARG224
D	ASP19
D	LYS23
D	TRP32
D	LMG411

site_id	AJ5
Number of Residues	6
Details	binding site for residue LMG D 411

Chain	Residue
B	ALA228
B	CLA608
B	CLA609
D	ARG134
D	LMG410
D	HOH525

site_id	AJ6
Number of Residues	9
Details	binding site for residue LHG E 101

Chain	Residue
A	TYR262
A	SER264
A	PHE265
A	ASN266
A	PL9409
D	PHE27
D	LMG407
E	PHE10
E	SER11

site_id	AJ7
Number of Residues	15
Details	binding site for residue HEM E 102

Chain	Residue
E	ILE13
E	ARG18
E	TYR19
E	ILE22
E	HIS23
E	THR26
E	LEU30
E	HOH210
F	ARG19
F	TRP20
F	VAL23
F	HIS24
F	ALA27
F	HOH204
R	ILE23

site_id	AJ8
Number of Residues	16
Details	binding site for residue SQD F 101

Chain	Residue
A	PL9409
D	ARG24
D	ARG26
E	HOH205
F	PHE16
F	THR17
F	VAL18
F	HOH205
R	GLN30
R	LEU34
R	HOH101
X	LEU23
X	VAL27
X	ILE31
X	ASP35
X	HOH101

site_id	AJ9
Number of Residues	6
Details	binding site for residue BCR H 101

Chain	Residue
B	CLA603
B	CLA609
H	PHE34
H	PHE38
H	PHE41
X	THR2

site_id	AK1
Number of Residues	15
Details	binding site for residue DGD H 102

Chain	Residue
B	TYR258
B	GLN274
B	SER277
B	CLA602
D	HIS87
D	LEU162
D	LEU291
H	TYR49
H	ASN50
H	VAL60
H	SER61
H	TRP62
H	HOH201
H	HOH206
H	HOH208

site_id	AK2
Number of Residues	13
Details	binding site for residue BCR K 101

Chain	Residue
C	PHE62
C	BCR520
J	ALA14
J	THR15
K	LEU31
K	ALA34
K	LEU35
K	PHE37
K	VAL38
Y	GLY29
Y	GLY32
Y	PRO33
Z	PHE17

site_id	AK3
Number of Residues	17
Details	binding site for residue LHG L 101

Chain	Residue
A	SER232
A	ASN234
B	PRO4
B	TRP5
B	TYR6
B	CLA614
B	LMG620
B	LHG622
D	TRP266
D	PHE273
D	PL9406
D	LHG408
L	GLU11
L	LEU12
L	ASN13
L	SER16
M	PHE21

site_id	AK4
Number of Residues	6
Details	binding site for residue BCR T 101

Chain	Residue
A	SQD412
T	PHE8
T	PHE18
b	TRP33
b	MET37
b	BCR619

site_id	AK5
Number of Residues	18
Details	binding site for residue HEC V 201

Chain	Residue
V	ALA36
V	CYS37
V	CYS40
V	HIS41
V	THR46
V	THR48
V	LEU52
V	ASP53
V	THR58
V	TYR75
V	TYR82
V	HIS92
V	HOH304
V	HOH324
V	HOH326
V	HOH329
V	HOH332
V	HOH334

site_id	AK6
Number of Residues	5
Details	binding site for residue FE2 a 401

Chain	Residue
a	HIS215
a	HIS272
a	BCT417
d	HIS214
d	HIS268

site_id	AK7
Number of Residues	6
Details	binding site for residue CL a 402

Chain	Residue
a	HOH557
d	LYS317
d	HOH573
a	ASN181
a	HIS332
a	GLU333

site_id	AK8
Number of Residues	3
Details	binding site for residue CL a 403

Chain	Residue
a	ASN338
a	PHE339
c	GLU354

site_id	AK9
Number of Residues	18
Details	binding site for residue CLA a 404

Chain	Residue
a	TYR147
a	PRO150
a	SER153
a	VAL157
a	MET183
a	PHE186
a	ILE192
a	HIS198
a	GLY201
a	PHE206
a	THR286
a	ALA287
a	ILE290
a	PHO406
d	LEU205
d	CLA402
d	CLA403
t	PHE17

site_id	AL1
Number of Residues	15
Details	binding site for residue CLA a 405

Chain	Residue
a	GLN199
a	VAL202
a	ALA203
a	GLY207
a	LEU210
a	TRP278
a	HOH514
a	HOH572
d	VAL175
d	ILE178
d	PHE179
d	LEU182
d	PHO401
d	CLA403
e	LHG101

site_id	AL2
Number of Residues	15
Details	binding site for residue PHO a 406

Chain	Residue
a	LEU41
a	ALA44
a	THR45
a	TYR126
a	GLN130
a	TYR147
a	GLY175
a	CLA404
d	ALA208
d	LEU209
d	ILE213
d	TRP253
d	PHE257
d	CLA402
d	LHG407

site_id	AL3
Number of Residues	12
Details	binding site for residue CLA a 407

Chain	Residue
a	THR40
a	PHE93
a	PRO95
a	ILE96
a	TRP97
a	LEU114
a	PHE117
a	HIS118
a	LMG414
i	TYR9
i	THR13
i	PHE15

site_id	AL4
Number of Residues	2
Details	binding site for residue BCR a 408

Chain	Residue
a	ALA43
a	ALA51

site_id	AL5
Number of Residues	17
Details	binding site for residue PL9 a 409

Chain	Residue
a	MET214
a	HIS215
a	LEU218
a	PHE255
a	ALA263
a	SER264
a	PHE265
d	VAL30
d	PHE38
d	PRO39
d	LEU45
d	PHO401
e	LHG101
f	ALA22
f	THR25
f	SQD101
x	THR24

site_id	AL6
Number of Residues	14
Details	binding site for residue LHG a 410

Chain	Residue
a	SER232
a	ASN234
a	HOH526
a	HOH562
b	TYR6
b	ARG7
b	TRP468
b	CLA612
b	CLA614
d	ARG139
d	TYR141
d	TRP266
d	PHE269
l	LHG101

site_id	AL7
Number of Residues	14
Details	binding site for residue SQD a 411

Chain	Residue
a	LEU200
a	ASN267
a	SER270
a	TRP278
a	VAL281
c	GLN28
c	ALA34
c	TRP36
c	HOH632
d	SER230
d	PHE232
d	ARG233
d	LHG408
k	PHE37

site_id	AL8
Number of Residues	7
Details	binding site for residue SQD a 412

Chain	Residue
B	CLA606
B	CLA616
B	BCR619
a	LEU28
a	LEU42
t	PHE22
t	BCR101

site_id	AL9
Number of Residues	5
Details	binding site for residue DGD a 413

Chain	Residue
B	TRP75
a	LEU102
a	ASP103
a	HOH571
o	LYS69

site_id	AM1
Number of Residues	13
Details	binding site for residue LMG a 414

Chain	Residue
a	PHE93
a	TRP97
a	GLU98
a	CLA407
a	HOH564
c	LEU214
c	PHE218
c	GLU221
c	TRP223
c	PHE284
c	CLA505
i	TYR9
i	HOH101

site_id	AM2
Number of Residues	17
Details	binding site for residue OEY a 416

Chain	Residue
a	ASP61
a	ASP170
a	VAL185
a	GLU189
a	HIS332
a	GLU333
a	HIS337
a	ASP342
a	ALA344
a	HOH508
a	HOH525
a	HOH530
a	HOH537
a	HOH563
a	HOH593
c	GLU354
c	ARG357

site_id	AM3
Number of Residues	10
Details	binding site for residue BCT a 417

Chain	Residue
a	HIS215
a	GLU244
a	TYR246
a	HIS272
a	FE2401
a	HOH509
d	HIS214
d	TYR244
d	LYS264
d	HIS268

site_id	AM4
Number of Residues	10
Details	binding site for residue SQD b 601

Chain	Residue
L	ARG14
L	TYR18
M	TYR26
T	CYS12
T	PHE23
b	ARG18
b	SER104
b	TRP115
b	CLA615
b	BCR618

site_id	AM5
Number of Residues	15
Details	binding site for residue CLA b 603

Chain	Residue
b	GLY189
b	PHE190
b	PRO192
b	ALA200
b	HIS201
b	PHE247
b	CLA604
b	CLA606
b	HOH837
d	ILE159
h	PHE38
h	ILE45
h	LEU46
h	TYR49
h	DGD103

site_id	AM6
Number of Residues	16
Details	binding site for residue CLA b 604

Chain	Residue
b	ARG68
b	LEU69
b	ALA146
b	CYS150
b	PHE153
b	HIS201
b	HIS202
b	THR262
b	CLA603
b	CLA605
b	CLA606
b	CLA607
b	CLA610
b	HOH769
h	MET35
h	PHE38

site_id	AM7
Number of Residues	18
Details	binding site for residue CLA b 605

Chain	Residue
b	TRP33
b	PHE61
b	PHE65
b	ARG68
b	VAL245
b	ALA248
b	VAL252
b	PHE451
b	HIS455
b	PHE458
b	PHE462
b	CLA604
b	CLA606
b	CLA608
b	CLA612
b	CLA613
b	CLA614
b	CLA616

site_id	AM8
Number of Residues	16
Details	binding site for residue CLA b 606

Chain	Residue
b	VAL30
b	ALA31
b	ALA34
b	VAL62
b	MET66
b	VAL96
b	HIS100
b	LEU103
b	LEU143
b	ALA205
b	CLA603
b	CLA604
b	CLA605
b	CLA607
b	CLA613
b	HOH734

site_id	AM9
Number of Residues	16
Details	binding site for residue CLA b 607

Chain	Residue
A	SQD412
A	DGD413
b	VAL71
b	TRP91
b	VAL96
b	ALA99
b	LEU149
b	GLY152
b	PHE153
b	PHE156
b	HIS157
b	PHE162
b	GLY163
b	PRO164
b	CLA604
b	CLA606

site_id	AN1
Number of Residues	17
Details	binding site for residue CLA b 608

Chain	Residue
b	TRP33
b	TYR40
b	GLN58
b	GLY59
b	PHE61
b	LEU324
b	THR327
b	GLY328
b	PRO329
b	TRP450
b	CLA605
b	CLA614
b	HOH853
d	MET281
l	PHE31
m	PHE14
m	LMG101

site_id	AN2
Number of Residues	15
Details	binding site for residue CLA b 609

Chain	Residue
b	LEU229
b	THR236
b	SER239
b	PHE463
b	HIS466
b	ILE467
b	CLA610
b	CLA611
b	HOH832
d	LEU36
d	PHE120
d	MET126
d	LEU127
d	CLA404
h	DGD103

site_id	AN3
Number of Residues	17
Details	binding site for residue CLA b 610

Chain	Residue
b	PHE139
b	ALA212
b	PHE215
b	HIS216
b	VAL219
b	PRO221
b	PRO222
b	LEU225
b	LEU229
b	CLA604
b	CLA609
b	CLA611
h	THR27
h	MET31
h	PHE34
h	LEU46
h	BCR102

site_id	AN4
Number of Residues	14
Details	binding site for residue CLA b 611

Chain	Residue
b	LEU135
b	PHE139
b	HIS142
b	LEU143
b	ALA146
b	MET231
b	VAL237
b	SER240
b	SER241
b	CLA609
b	CLA610
b	CLA613
b	HOH745
h	BCR102

site_id	AN5
Number of Residues	15
Details	binding site for residue CLA b 612

Chain	Residue
a	LHG410
a	HOH562
b	TYR6
b	ARG7
b	VAL8
b	HIS9
b	LEU238
b	PHE462
b	GLY465
b	TRP468
b	HIS469
b	ARG472
b	CLA605
b	CLA613
b	CLA614

site_id	AN6
Number of Residues	16
Details	binding site for residue CLA b 613

Chain	Residue
b	HIS9
b	LEU19
b	HIS23
b	HIS26
b	THR27
b	VAL237
b	LEU238
b	SER241
b	CLA605
b	CLA606
b	CLA611
b	CLA612
b	CLA614
b	CLA615
b	CLA616
b	HOH773

site_id	AN7
Number of Residues	12
Details	binding site for residue CLA b 614

Chain	Residue
a	LHG410
b	HIS9
b	HIS26
b	PHE462
b	CLA605
b	CLA608
b	CLA612
b	CLA613
b	CLA615
b	BCR618
b	BCR619
m	LMG101

site_id	AN8
Number of Residues	11
Details	binding site for residue CLA b 615

Chain	Residue
b	VAL8
b	HIS9
b	LEU29
b	SQD601
b	CLA613
b	CLA614
b	BCR618
l	GLN8
m	LEU13
m	PHE21
m	LMG101

site_id	AN9
Number of Residues	11
Details	binding site for residue CLA b 616

Chain	Residue
b	HIS23
b	LEU24
b	MET138
b	ILE141
b	HIS142
b	LEU145
b	CLA605
b	CLA613
b	CLA617
b	BCR620
h	LEU14

site_id	AO1
Number of Residues	11
Details	binding site for residue CLA b 617

Chain	Residue
A	SQD412
b	LEU24
b	ALA110
b	TRP113
b	HIS114
b	CLA616
b	BCR620
b	HOH811
h	THR5
h	LEU7
h	LEU11

site_id	AO2
Number of Residues	6
Details	binding site for residue BCR b 618

Chain	Residue
b	MET25
b	TRP115
b	SQD601
b	CLA614
b	CLA615
b	BCR619

site_id	AO3
Number of Residues	8
Details	binding site for residue BCR b 619

Chain	Residue
T	BCR101
b	GLY32
b	SER36
b	ILE101
b	VAL102
b	GLY105
b	CLA614
b	BCR618

site_id	AO4
Number of Residues	4
Details	binding site for residue BCR b 620

Chain	Residue
A	SQD412
b	TYR117
b	CLA616
b	CLA617

site_id	AO5
Number of Residues	8
Details	binding site for residue LMG b 622

Chain	Residue
b	THR159
b	ALA182
b	TRP185
b	ILE207
b	HOH800
c	LEU204
c	LEU253
c	HOH670

site_id	AO6
Number of Residues	6
Details	binding site for residue LMG b 623

Chain	Residue
b	ARG224
b	LEU225
b	ALA228
d	TRP32
d	CLA404
h	ALA32

site_id	AO7
Number of Residues	15
Details	binding site for residue CLA c 501

Chain	Residue
c	LEU95
c	LEU168
c	GLY171
c	ALA172
c	HIS237
c	ALA278
c	MET282
c	PHE289
c	VAL296
c	TYR297
c	CLA502
c	CLA503
c	CLA506
c	BCR515
c	HOH704

site_id	AO8
Number of Residues	14
Details	binding site for residue CLA c 502

Chain	Residue
c	TRP63
c	LEU88
c	HIS91
c	LEU95
c	MET282
c	ALA286
c	TYR297
c	HIS430
c	LEU433
c	PHE437
c	CLA501
c	CLA503
c	CLA510
c	CLA512

site_id	AO9
Number of Residues	12
Details	binding site for residue CLA c 503

Chain	Residue
c	ILE60
c	VAL61
c	ALA64
c	THR68
c	LEU88
c	HIS91
c	HIS118
c	CLA501
c	CLA502
c	CLA510
c	CLA512
c	CLA513

site_id	AP1
Number of Residues	15
Details	binding site for residue CLA c 504

Chain	Residue
c	TRP63
c	PHE70
c	GLY85
c	ILE87
c	TRP425
c	SER429
c	HIS430
c	CLA508
c	CLA510
c	DGD517
c	LMG519
c	HOH673
c	HOH713
k	PRO26
k	VAL30

site_id	AP2
Number of Residues	11
Details	binding site for residue CLA c 505

Chain	Residue
a	TRP131
a	LMG414
c	PHE264
c	TYR274
c	HIS441
c	LEU442
c	ALA445
c	ARG449
c	CLA507
c	BCR515
c	HOH623

site_id	AP3
Number of Residues	15
Details	binding site for residue CLA c 506

Chain	Residue
c	LEU161
c	LEU165
c	LEU213
c	GLY247
c	TRP250
c	HIS251
c	THR254
c	PRO256
c	PHE257
c	TRP259
c	ALA260
c	PHE264
c	CLA501
c	CLA507
c	BCR515

site_id	AP4
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	ALA278
c	MET282
c	CLA505
c	CLA506
c	CLA509
c	HOH652

site_id	AP5
Number of Residues	15
Details	binding site for residue CLA c 508

Chain	Residue
c	TRP36
c	ALA37
c	GLY38
c	ASN39
c	LEU272
c	LEU276
c	PHE436
c	TRP443
c	HIS444
c	ARG447
c	CLA504
c	CLA509
c	CLA510
c	DGD518
d	LHG408

site_id	AP6
Number of Residues	16
Details	binding site for residue CLA c 509

Chain	Residue
c	ASN39
c	LEU49
c	ALA52
c	HIS53
c	HIS56
c	TRP151
c	GLY268
c	GLU269
c	TYR271
c	LEU272
c	SER275
c	CLA507
c	CLA508
c	CLA510
c	CLA511
c	CLA512

site_id	AP7
Number of Residues	14
Details	binding site for residue CLA c 510

Chain	Residue
c	ASN39
c	HIS56
c	LEU59
c	LEU279
c	PHE437
c	CLA502
c	CLA503
c	CLA504
c	CLA508
c	CLA509
c	CLA511
c	LMG519
k	PRO29
k	LEU33

site_id	AP8
Number of Residues	20
Details	binding site for residue CLA c 511

Chain	Residue
c	THR24
c	ARG26
c	TRP35
c	GLY38
c	ASN39
c	ARG41
c	LEU42
c	LYS48
c	GLY126
c	PHE127
c	ILE134
c	CLA509
c	CLA510
c	BCR521
k	LEU33
k	TRP39
k	GLN40
y	ILE36
y	LEU46
z	VAL20

site_id	AP9
Number of Residues	13
Details	binding site for residue CLA c 512

Chain	Residue
c	HIS53
c	PHE147
c	ILE160
c	PHE163
c	HIS164
c	ILE166
c	VAL167
c	GLY171
c	CLA502
c	CLA503
c	CLA509
c	CLA513
c	BCR514

site_id	AQ1
Number of Residues	12
Details	binding site for residue CLA c 513

Chain	Residue
c	VAL124
c	GLY128
c	TYR131
c	HIS132
c	PRO137
c	LEU140
c	TYR143
c	PHE147
c	CLA503
c	CLA512
c	BCR514
c	HOH684

site_id	AQ2
Number of Residues	6
Details	binding site for residue BCR c 514

Chain	Residue
c	SER121
c	VAL124
c	CLA512
c	CLA513
k	TYR15
z	VAL51

site_id	AQ3
Number of Residues	8
Details	binding site for residue BCR c 515

Chain	Residue
c	ILE209
c	LEU213
c	ILE224
c	PHE264
c	CLA501
c	CLA505
c	CLA506
i	PHE23

site_id	AQ4
Number of Residues	19
Details	binding site for residue DGD c 516

Chain	Residue
a	PHE155
a	ILE160
a	ILE163
c	PRO217
c	GLY219
c	GLY220
c	GLU221
c	GLY222
c	TRP223
c	PHE292
c	ASN293
c	ASN294
c	THR295
c	ASP360
c	PHE361
c	ARG362
c	LEU438
c	HOH648
c	HOH677

site_id	AQ5
Number of Residues	17
Details	binding site for residue DGD c 517

Chain	Residue
a	HIS195
c	GLU83
c	GLN84
c	GLY85
c	SER406
c	ASN418
c	PHE419
c	VAL420
c	TRP425
c	CLA504
c	DGD518
c	LMG519
c	HOH606
c	HOH706
c	HOH710
d	LMG409
j	TYR33

site_id	AQ6
Number of Residues	19
Details	binding site for residue DGD c 518

Chain	Residue
a	LEU200
a	ALA203
a	ASN301
a	SER305
c	ASN405
c	VAL407
c	ASN415
c	SER416
c	ASN418
c	CLA508
c	DGD517
c	HOH615
j	ALA32
j	TYR33
j	GLY37
j	SER38
j	SER39
j	HOH203
v	GLN34

site_id	AQ7
Number of Residues	6
Details	binding site for residue LMG c 519

Chain	Residue
c	HIS74
c	CLA504
c	CLA510
c	DGD517
k	ASP23
y	GLN21

site_id	AQ8
Number of Residues	9
Details	binding site for residue BCR c 521

Chain	Residue
c	GLY58
c	LEU59
c	VAL116
c	SER122
c	CLA511
k	PHE32
k	LEU35
y	BCR101
z	SER16

site_id	AQ9
Number of Residues	8
Details	binding site for residue LMG c 522

Chain	Residue
b	PRO183
b	GLU184
b	TRP185
c	LEU204
c	LEU242
c	ILE245
c	HOH670
h	CLA101

site_id	AR1
Number of Residues	16
Details	binding site for residue PHO d 401

Chain	Residue
a	PHE206
a	LEU210
a	MET214
a	CLA405
a	PL9409
d	LEU45
d	TRP48
d	GLY121
d	LEU122
d	PHE125
d	GLN129
d	ASN142
d	ALA145
d	PHE146
d	PHE153
d	CLA403

site_id	AR2
Number of Residues	14
Details	binding site for residue CLA d 402

Chain	Residue
a	PHE158
a	ILE176
a	THR179
a	MET183
a	CLA404
a	PHO406
d	MET198
d	VAL201
d	ALA202
d	CLA403
d	PL9406
d	HOH525
d	HOH590
l	LHG101

site_id	AR3
Number of Residues	17
Details	binding site for residue CLA d 403

Chain	Residue
a	MET183
a	PHE206
a	CLA404
a	CLA405
d	PRO149
d	VAL152
d	VAL156
d	PHE185
d	TRP191
d	THR192
d	HIS197
d	GLY200
d	SER282
d	ALA283
d	VAL286
d	PHO401
d	CLA402

site_id	AR4
Number of Residues	20
Details	binding site for residue CLA d 404

Chain	Residue
b	CLA609
b	LMG623
d	ILE35
d	CYS40
d	LEU43
d	LEU89
d	LEU90
d	LEU91
d	LEU92
d	TRP93
d	THR112
d	PHE113
d	LEU116
d	HIS117
h	ALA32
h	GLY36
h	LEU43
h	HOH202
x	LEU14
x	VAL20

site_id	AR5
Number of Residues	9
Details	binding site for residue BCR d 405

Chain	Residue
d	TYR42
d	GLY46
d	GLY47
d	LEU49
d	THR50
d	LMG409
f	PRO29
f	THR30
f	PHE33

site_id	AR6
Number of Residues	13
Details	binding site for residue PL9 d 406

Chain	Residue
a	ILE77
d	MET199
d	ALA202
d	HIS214
d	THR217
d	MET246
d	TRP253
d	ALA260
d	PHE261
d	LEU267
d	CLA402
l	LHG101
t	PHE10

site_id	AR7
Number of Residues	15
Details	binding site for residue LHG d 407

Chain	Residue
a	PHO406
d	ILE256
d	ALA260
d	PHE261
d	SER262
d	ASN263
d	TRP266
d	HOH539
l	ASN13
l	THR15
l	LEU19
l	LHG101
l	HOH204
t	ALA20
t	ILE21

site_id	AR8
Number of Residues	13
Details	binding site for residue LHG d 408

Chain	Residue
a	ARG140
a	TRP142
a	PHE273
a	SQD411
c	TRP443
c	ARG447
c	CLA508
d	GLU219
d	ASN220
d	ALA229
d	THR231
d	PHE232
d	HOH589

site_id	AR9
Number of Residues	15
Details	binding site for residue LMG d 409

Chain	Residue
c	DGD517
d	TYR67
d	GLY70
d	CYS71
d	ASN72
d	PHE73
d	BCR405
f	THR30
f	MET40
f	GLN41
j	PHE28
j	GLY31
j	ALA32
j	LEU36
j	HOH201

site_id	AS1
Number of Residues	7
Details	binding site for residue LHG e 101

Chain	Residue
a	PHE260
a	TYR262
a	CLA405
a	PL9409
d	PHE27
e	PHE10
e	SER11

site_id	AS2
Number of Residues	14
Details	binding site for residue HEM e 102

Chain	Residue
e	ARG8
e	ILE13
e	ARG18
e	TYR19
e	HIS23
e	LEU30
e	HOH209
f	ILE15
f	ARG19
f	TRP20
f	HIS24
f	ALA27
f	ILE31
r	ALA19

site_id	AS3
Number of Residues	9
Details	binding site for residue SQD f 101

Chain	Residue
a	PL9409
d	ARG24
d	ARG26
e	HOH206
f	PHE16
f	THR17
f	VAL18
x	VAL27
x	ASP35

site_id	AS4
Number of Residues	8
Details	binding site for residue CLA h 101

Chain	Residue
b	TRP185
b	PRO187
b	PHE190
b	HOH767
c	PHE181
c	LMG522
h	PHE41
h	BCR102

site_id	AS5
Number of Residues	12
Details	binding site for residue BCR h 102

Chain	Residue
b	CLA610
b	CLA611
h	PHE34
h	MET35
h	LEU37
h	PHE38
h	PHE41
h	ILE44
h	LEU55
h	CLA101
x	THR2
x	LEU7

site_id	AS6
Number of Residues	23
Details	binding site for residue DGD h 103

Chain	Residue
b	TYR193
b	PHE250
b	TYR258
b	TYR273
b	GLN274
b	SER277
b	PHE463
b	CLA603
b	CLA609
b	HOH730
d	HIS87
d	LEU162
d	GLY163
d	LEU291
d	HOH516
h	LEU46
h	TYR49
h	ASN50
h	VAL60
h	SER61
h	TRP62
h	HOH205
h	HOH211

site_id	AS7
Number of Residues	16
Details	binding site for residue LHG l 101

Chain	Residue
a	SER232
a	ASN234
a	LHG410
b	PRO4
b	TRP5
b	TYR6
d	TRP266
d	PHE273
d	CLA402
d	PL9406
d	LHG407
l	GLU11
l	LEU12
l	ASN13
l	SER16
m	PHE21

site_id	AS8
Number of Residues	8
Details	binding site for residue LMG m 101

Chain	Residue
b	TYR40
b	THR327
b	CLA608
b	CLA614
b	CLA615
l	PHE35
m	ASN4
m	LEU6

site_id	AS9
Number of Residues	7
Details	binding site for residue BCR t 101

Chain	Residue
B	TRP33
B	BCR618
a	SQD412
t	PHE8
t	ALA11
t	ALA15
t	PHE18

site_id	AT1
Number of Residues	10
Details	binding site for residue BCR y 101

Chain	Residue
c	PHE62
c	BCR521
k	LEU21
k	LEU31
k	ALA34
k	VAL38
y	ILE28
y	GLY29
z	SER16
z	PHE17

site_id	AT2
Number of Residues	20
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	ASP53
v	THR58
v	LEU59
v	TYR75
v	TYR82
v	ILE88
v	HIS92
v	HOH305
v	HOH322
v	HOH330

site_id	AT3
Number of Residues	18
Details	binding site for Di-peptide HEM v 201 and CYS v 37

Chain	Residue
v	PHE33
v	ALA36
v	ALA38
v	SER39
v	CYS40
v	HIS41
v	THR46
v	THR48
v	ASP53
v	THR58
v	LEU59
v	TYR75
v	TYR82
v	ILE88
v	HIS92
v	HOH305
v	HOH322
v	HOH330

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
D	ASN190-ALA216
A	ASN191-SER217

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	442
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	218
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)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)