Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2AXT

Crystal Structure of Photosystem II from Thermosynechococcus elongatus

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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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	3
Details	BINDING SITE FOR RESIDUE CA K 56

Chain	Residue
K	ASP19
K	ASP23
X	UNK2

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 A 557

Chain	Residue
A	HIS215
A	HIS272
D	HIS214
D	HIS268
D	BCT353

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BCT D 353

Chain	Residue
A	GLU244
A	TYR246
A	HIS272
A	FE2557
D	HIS214
D	TYR244
D	LYS264
D	HIS268
A	HIS215

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA k 5056

Chain	Residue
k	ASP5019
k	ASP5023
x	UNK5002

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 a 5557

Chain	Residue
a	HIS5215
a	HIS5272
d	HIS5214
d	HIS5268
d	BCT5353

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BCT d 5353

Chain	Residue
a	HIS5215
a	GLU5244
a	TYR5246
a	HIS5272
a	FE25557
d	HIS5214
d	TYR5244
d	LYS5264
d	HIS5268

site_id	AC7
Number of Residues	20
Details	BINDING SITE FOR RESIDUE CLA A 558

Chain	Residue
A	PHE119
A	TYR147
A	PRO150
A	SER153
A	VAL157
A	MET183
A	ILE184
A	PHE186
A	GLN187
A	LEU193
A	HIS198
A	GLY201
A	VAL205
A	THR286
A	ILE290
A	CLA559
A	CLA560
A	PHO561
D	CLA354
D	MGE360

site_id	AC8
Number of Residues	23
Details	BINDING SITE FOR RESIDUE CLA D 354

Chain	Residue
A	MET183
A	PHE206
A	CLA558
A	CLA559
A	CLA560
A	PHO562
D	VAL152
D	VAL156
D	PHE181
D	LEU182
D	PHE185
D	GLN186
D	TRP191
D	THR192
D	HIS197
D	GLY200
D	VAL201
D	VAL204
D	LEU279
D	SER282
D	ALA283
D	VAL286
D	MGE358

site_id	AC9
Number of Residues	18
Details	BINDING SITE FOR RESIDUE CLA A 559

Chain	Residue
A	THR45
A	VAL157
A	PHE158
A	MET172
A	ILE176
A	THR179
A	PHE180
A	MET183
A	CLA558
A	PHO561
C	UNL474
D	MET198
D	VAL201
D	ALA202
D	GLY206
D	LEU209
D	CLA354
L	MGE210

site_id	BC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLA A 560

Chain	Residue
A	LEU210
A	TRP278
A	CLA558
A	PHO562
C	DGD509
D	PHE157
D	VAL175
D	PHE179
D	LEU182
D	CLA354
A	GLN199
A	VAL202
A	ALA203
A	GLY207

site_id	BC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE PHO A 561

Chain	Residue
A	LEU41
A	ALA44
A	THR45
A	ILE115
A	PHE119
A	TYR126
A	GLN130
A	TYR147
A	PRO150
A	PHE158
A	LEU174
A	PRO279
A	VAL283
A	CLA558
A	CLA559
D	LEU205
D	ALA208
D	LEU209
D	ILE213
D	TRP253
D	PHE257

site_id	BC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE PHO A 562

Chain	Residue
A	PHE206
A	ALA209
A	LEU210
A	ALA213
A	MET214
A	LEU258
A	CLA560
D	LEU37
D	ALA41
D	LEU45
D	TRP48
D	LEU122
D	PHE125
D	GLN129
D	ASN142
D	PHE146
D	PRO149
D	PHE153
D	PRO275
D	LEU279
D	CLA354

site_id	BC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLA A 563

Chain	Residue
A	ILE36
A	PRO39
A	PHE93
A	PRO95
A	ILE96
A	TRP97
A	LEU114
A	PHE117
A	HIS118
I	TYR9
I	VAL12
I	THR13
I	PHE15
I	MGE201

site_id	BC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE CLA D 355

Chain	Residue
C	UNL480
D	LEU36
D	PRO39
D	LEU43
D	LEU89
D	LEU90
D	LEU91
D	LEU92
D	TRP93
D	THR112
D	PHE113
D	HIS117
D	PHE120
D	BCR357
X	UNK63
X	UNK64
X	UNK67

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CLA B 511

Chain	Residue
B	TRP185
B	PHE190
B	CLA512
H	PHE41
H	BCR107

site_id	BC7
Number of Residues	19
Details	BINDING SITE FOR RESIDUE CLA B 512

Chain	Residue
B	GLY189
B	PHE190
B	GLY197
B	ALA200
B	HIS201
B	ALA204
B	ALA205
B	VAL208
B	PHE247
B	PHE250
B	CLA511
B	CLA513
B	CLA518
D	LEU158
D	ILE159
H	PHE38
H	ILE45
H	LEU46
H	TYR49

site_id	BC8
Number of Residues	18
Details	BINDING SITE FOR RESIDUE CLA B 513

Chain	Residue
B	ARG68
B	LEU69
B	ALA146
B	LEU149
B	CYS150
B	PHE153
B	LEU158
B	HIS201
B	HIS202
B	PHE247
B	VAL252
B	THR262
B	CLA512
B	CLA514
B	CLA515
B	CLA516
H	PHE38
H	LEU39

site_id	BC9
Number of Residues	19
Details	BINDING SITE FOR RESIDUE CLA B 514

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	PHE462
B	CLA513
B	CLA515
B	CLA517
B	CLA522
B	CLA523
B	CLA525

site_id	CC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE CLA B 515

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	GLY147
B	ALA205
B	CLA513
B	CLA514
B	CLA516
B	CLA520

site_id	CC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CLA B 516

Chain	Residue
B	LEU69
B	GLY70
B	TRP91
B	ALA99
B	HIS100
B	LEU103
B	GLY152
B	PHE153
B	PHE156
B	HIS157
B	PHE162
B	GLY163
B	PRO164
B	CLA513
B	CLA515
B	BCR529

site_id	CC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE CLA B 517

Chain	Residue
B	TRP33
B	TYR40
B	GLN58
B	GLY59
B	PHE61
B	LEU324
B	PHE325
B	THR327
B	GLY328
B	PRO329
B	TRP450
B	PHE451
B	HIS455
B	CLA514
B	MGE530
D	PHE196
D	MET281
L	LEU27
M	PHE14
t	BCR104

site_id	CC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE CLA B 518

Chain	Residue
B	THR236
B	SER239
B	ALA243
B	PHE246
B	PHE463
B	HIS466
B	LEU474
B	CLA512
B	CLA519
B	CLA520
C	UNL481
C	UNL482
D	ILE123
D	MET126
D	LEU127
D	PHE130
H	LEU43
H	LEU46

site_id	CC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CLA B 519

Chain	Residue
B	PHE139
B	ALA212
B	PHE215
B	HIS216
B	PRO221
B	LEU229
B	CLA518
B	CLA520
H	THR27
H	THR28
H	MET31
H	PHE34
H	BCR107

site_id	CC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CLA B 520

Chain	Residue
B	LEU135
B	PRO136
B	PHE139
B	HIS142
B	MET231
B	VAL237
B	SER240
B	SER241
B	CLA515
B	CLA518
B	CLA519
B	CLA522
B	CLA525

site_id	CC7
Number of Residues	19
Details	BINDING SITE FOR RESIDUE CLA B 521

Chain	Residue
B	TRP5
B	TYR6
B	ARG7
B	VAL8
B	HIS9
B	LEU238
B	ILE242
B	LEU461
B	PHE462
B	PHE464
B	GLY465
B	TRP468
B	HIS469
B	ARG472
B	PHE479
B	CLA522
B	CLA523
B	CLA524
D	MGE359

site_id	CC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CLA B 522

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	CLA514
B	CLA520
B	CLA521
B	CLA523
B	CLA525

site_id	CC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CLA B 523

Chain	Residue
B	HIS9
B	HIS26
B	VAL30
B	PHE462
B	CLA514
B	CLA521
B	CLA522
B	CLA524
B	BCR527
B	BCR528
D	MGE359

site_id	DC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CLA B 524

Chain	Residue
B	VAL8
B	HIS9
B	LEU12
B	ALA22
B	MET25
B	LEU29
B	TRP115
B	CLA521
B	CLA523
B	BCR527
L	ARG7
L	VAL10
L	MGE210
c	UNL5475
c	UNL5476

site_id	DC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CLA B 525

Chain	Residue
B	ILE20
B	HIS23
B	MET138
B	ILE141
B	HIS142
B	LEU145
B	CLA514
B	CLA520
B	CLA522
B	CLA526
H	LEU14

site_id	DC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CLA B 526

Chain	Residue
B	ILE20
B	LEU24
B	ALA110
B	TRP113
B	HIS114
B	LEU120
B	CLA525
H	THR5
H	LEU7

site_id	DC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CLA C 491

Chain	Residue
C	LEU95
C	LEU168
C	GLY171
C	ALA172
C	ILE224
C	VAL233
C	HIS237
C	ILE240
C	ALA278
C	MET281
C	MET282
C	VAL296
C	TYR297
C	CLA492
C	CLA493
C	BCR506

site_id	DC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLA C 492

Chain	Residue
C	TRP63
C	HIS91
C	GLY171
C	LEU175
C	LYS178
C	ALA286
C	TYR297
C	HIS430
C	LEU433
C	PHE437
C	CLA491
C	CLA493
C	CLA494
C	CLA500

site_id	DC6
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CLA C 493

Chain	Residue
C	ILE60
C	VAL61
C	ALA64
C	THR68
C	LEU88
C	HIS91
C	ILE92
C	LEU95
C	VAL114
C	HIS118
C	LEU279
C	UNL477
C	CLA491
C	CLA492
C	CLA500
C	CLA502

site_id	DC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLA C 494

Chain	Residue
C	TRP63
C	MET67
C	PHE70
C	GLY85
C	ILE87
C	SER406
C	TRP425
C	SER429
C	HIS430
C	UNL478
C	CLA492
C	CLA500
C	DGD508
K	PRO26

site_id	DC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CLA C 495

Chain	Residue
A	ILE36
A	SER124
A	MET127
A	TRP131
C	ILE265
C	TYR274
C	GLY277
C	ALA278
C	LEU438
C	HIS441
C	LEU442
C	ALA445
C	ARG449
C	CLA497
I	PHE23

site_id	DC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CLA C 496

Chain	Residue
C	LEU165
C	ILE243
C	GLY247
C	TRP250
C	HIS251
C	PRO256
C	PHE257
C	TRP259
C	PHE264
C	CLA497
C	BCR506
I	LEU24

site_id	EC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLA C 497

Chain	Residue
C	MET157
C	LEU161
C	HIS164
C	LEU168
C	PHE264
C	TRP266
C	TYR271
C	TYR274
C	SER275
C	LEU279
C	MET282
C	CLA495
C	CLA496
C	CLA499

site_id	EC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CLA C 498

Chain	Residue
A	LHG567
C	TRP36
C	ALA37
C	ASN39
C	ALA40
C	GLU269
C	LEU276
C	PHE436
C	PHE437
C	GLY440
C	TRP443
C	HIS444
C	ARG447
C	CLA499
C	CLA500

site_id	EC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CLA C 499

Chain	Residue
C	ASN39
C	LEU49
C	ALA52
C	HIS53
C	HIS56
C	GLY268
C	GLU269
C	SER275
C	CLA497
C	CLA498
C	CLA500

site_id	EC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CLA C 500

Chain	Residue
C	ASN39
C	HIS56
C	LEU59
C	LEU279
C	PHE436
C	PHE437
C	CLA492
C	CLA493
C	CLA494
C	CLA498
C	CLA499
C	CLA501
K	PRO29
K	VAL30
K	LEU33

site_id	EC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE CLA C 501

Chain	Residue
C	ASP27
C	TRP35
C	GLY38
C	ASN39
C	ARG41
C	LEU42
C	LEU45
C	LYS48
C	ALA52
C	PHE127
C	ALA133
C	ILE134
C	CLA500
C	BCR504
K	TRP39
K	GLN40
X	UNK31
Z	VAL20
Z	PRO24

site_id	EC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CLA C 502

Chain	Residue
C	HIS53
C	PHE147
C	PHE163
C	HIS164
C	VAL167
C	LEU168
C	GLY171
C	CLA493
C	CLA503
C	BCR505

site_id	EC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CLA C 503

Chain	Residue
C	LEU50
C	GLY128
C	TYR131
C	HIS132
C	PRO137
C	LEU140
C	PHE147
C	CLA502
C	BCR505

site_id	EC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEM F 51

Chain	Residue
E	ILE13
E	ARG18
E	TYR19
E	HIS23
E	THR26
E	ILE27
F	ARG19
F	TRP20
F	HIS24
F	ALA27
F	ILE31
X	UNK116

site_id	EC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEM V 552

Chain	Residue
V	ALA62
V	CYS63
V	CYS66
V	HIS67
V	THR74
V	LEU78
V	ASP79
V	LEU80
V	THR84
V	TYR101
V	TYR108
V	HIS118

site_id	FC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PQ9 D 356

Chain	Residue
C	UNL474
D	LEU209
D	LEU210
D	HIS214
D	THR217
D	ASN250
D	TRP253
D	ALA260
D	PHE261
D	LEU267
D	PHE270
D	VAL274

site_id	FC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PQ9 A 564

Chain	Residue
A	HIS215
A	LEU218
A	ALA251
A	HIS252
A	PHE255
A	SER264
A	PHE265
A	LEU271
A	PHE274

site_id	FC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE OEC A 565

Chain	Residue
A	ASP170
A	GLU189
A	HIS332
A	GLU333
A	ASP342
A	ALA344
C	GLU354

site_id	FC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BCR A 566

Chain	Residue
A	ILE38
A	ALA43
A	ALA51
A	ALA54
A	TRP105
I	PHE15

site_id	FC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE BCR B 527

Chain	Residue
B	MET25
B	LEU29
B	TRP115
B	CLA523
B	CLA524
B	BCR528
B	MGE530
M	ALA10
t	BCR104
t	PHE5019

site_id	FC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE BCR t 104

Chain	Residue
B	TRP33
B	SER36
B	MET37
B	LEU109
B	CLA517
B	BCR527
B	BCR528
a	SQD212
t	ILE5004
t	PHE5008
t	ALA5011
t	PHE5018
t	PHE5022

site_id	FC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BCR B 528

Chain	Residue
B	LEU29
B	GLY32
B	TRP33
B	SER36
B	ILE101
B	VAL102
B	CLA523
B	BCR527
t	BCR104

site_id	FC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BCR B 529

Chain	Residue
B	LEU106
B	CYS112
B	VAL116
B	TYR117
B	CLA516
a	SQD212

site_id	FC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BCR H 107

Chain	Residue
B	CLA511
B	CLA519
H	MET35
H	PHE38
H	PHE41
X	UNK52
X	UNK57

site_id	GC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE BCR D 357

Chain	Residue
D	TYR42
D	LEU43
D	GLY46
D	GLY47
D	LEU49
D	THR50
D	PHE113
D	CLA355
F	PRO29
F	THR30
F	PHE33
F	ILE37
J	VAL21
J	VAL25

site_id	GC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE BCR X 130

Chain	Residue
C	BCR504
J	ALA14
J	THR15
J	GLY18
J	MET19
K	LEU21
K	LEU31
K	ALA34
K	PHE37
K	VAL38
X	UNK13
X	UNK14
X	UNK17
Z	VAL13

site_id	GC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE BCR C 504

Chain	Residue
C	ALA55
C	GLY58
C	LEU59
C	VAL116
C	LEU119
C	SER122
C	ALA123
C	GLY126
C	CLA501
C	BCR505
K	TYR15
K	PHE18
K	PHE32
K	ALA36
X	BCR130

site_id	GC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE BCR C 505

Chain	Residue
C	PHE112
C	VAL116
C	ILE120
C	SER121
C	VAL124
C	LEU125
C	CLA502
C	CLA503
C	BCR504
K	TYR15
Z	GLY55

site_id	GC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE BCR C 506

Chain	Residue
C	ILE209
C	TYR212
C	LEU213
C	ILE224
C	VAL227
C	ASP232
C	VAL233
C	HIS237
C	PHE264
C	CLA491
C	CLA496
I	VAL20
I	PHE23
I	LEU24

site_id	GC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE MGE I 201

Chain	Residue
A	PHE93
A	TRP97
A	LEU121
A	CLA563
C	SER216
C	PHE218
C	TRP223
C	MET281
C	PHE284
I	LYS5
I	TYR9

site_id	GC7
Number of Residues	17
Details	BINDING SITE FOR RESIDUE DGD C 507

Chain	Residue
A	PHE155
A	ILE160
A	ILE163
C	PRO217
C	PHE218
C	GLY219
C	GLY220
C	GLY222
C	VAL225
C	SER226
C	ASN228
C	PHE284
C	CYS288
C	PHE292
C	ASN294
C	ARG362
C	LEU438

site_id	GC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE LHG A 567

Chain	Residue
A	ARG140
A	TRP142
A	PHE273
A	SQD568
C	TRP36
C	PHE436
C	TRP443
C	ARG447
C	CLA498
D	GLU219
D	ASN220
D	ALA229
D	SER230
D	THR231
D	PHE232

site_id	GC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SQD A 568

Chain	Residue
A	ASN267
A	SER270
A	PHE273
A	PHE274
A	LHG567
C	GLU29
C	TRP36
D	SER230
D	PHE232
D	ARG233

site_id	HC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE DGD C 508

Chain	Residue
A	PHE197
C	GLU83
C	GLN84
C	GLY85
C	SER406
C	ASN418
C	PHE419
C	VAL420
C	TRP425
C	THR428
C	UNL479
C	CLA494
C	DGD509
J	TYR33

site_id	HC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE DGD C 509

Chain	Residue
A	GLN199
A	LEU200
A	PHE300
A	ASN301
A	PHE302
A	SER305
A	CLA560
C	ASN405
C	ASN415
C	SER416
C	ASN418
C	DGD508
D	MGE358
J	PHE29
J	ALA32
J	TYR33
J	GLY37
J	SER38
J	SER39
V	GLN60

site_id	HC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE MGE D 358

Chain	Residue
C	DGD509
D	TYR67
D	GLY70
D	CYS71
D	CLA354
F	THR30
F	MET40
F	GLN41
J	GLY31
J	ALA32
J	GLY35
J	GLY37

site_id	HC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE DGD H 208

Chain	Residue
B	TYR193
B	PHE250
B	TYR258
B	TYR273
B	SER277
B	PHE463
D	HIS87
D	ILE123
D	LEU162
D	SER165
H	TYR49
H	VAL60
H	SER61
H	TRP62

site_id	HC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE MGE D 359

Chain	Residue
A	ASN234
B	TRP5
B	TYR6
B	ARG7
B	PHE464
B	TRP468
B	CLA521
B	CLA523
D	ARG139
D	TYR141
D	PHE269
D	PHE273
L	MGE210

site_id	HC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE MGE L 210

Chain	Residue
A	SER232
A	ASN234
A	CLA559
B	TRP5
B	TYR6
B	CLA524
C	UNL474
D	TRP266
D	PHE270
D	PHE273
D	MGE359
L	GLU11
L	SER16
L	GLY20

site_id	HC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE MGE D 360

Chain	Residue
A	CLA558
D	ILE259
D	ALA260
D	PHE261
D	SER262
D	ASN263
D	TRP266
D	PHE270
L	THR15
L	TYR18
L	LEU19
T	PHE10
T	PHE17
T	ALA20

site_id	HC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SQD a 212

Chain	Residue
B	TRP113
B	TYR117
B	BCR529
a	TRP5020
a	ASN5026
a	ARG5027
a	LEU5028
t	BCR104

site_id	HC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SQD t 213

Chain	Residue
B	ARG18
B	LEU29
B	SER104
l	ARG5014
l	TYR5018
t	PHE5019
t	PHE5023

site_id	IC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MGE B 530

Chain	Residue
B	THR327
B	GLY328
B	PRO329
B	PHE453
B	CLA517
B	BCR527
L	PHE35
M	ASN4
M	LEU6
M	LMT5216

site_id	IC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE LMT A 569

Chain	Residue
A	ILE50
A	LEU72
A	TYR73
C	UNL488
C	UNL489
D	ARG304
O	GLY139
O	GLU140
T	LMT217
b	ALA5043
b	LEU5098

site_id	IC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE LMT m 216

Chain	Residue
M	MET1
M	LMT5216
T	MET1
T	ILE4
T	LMT217
b	TYR5040
b	MGE5530
m	GLN5005
m	LEU5006

site_id	IC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE LMT T 217

Chain	Residue
A	LEU72
A	LMT569
T	MET1
T	ILE4
T	ALA11
T	ILE14
b	TYR5040
b	ALA5043
b	THR5044
b	BCR5528
m	LMT216

site_id	IC5
Number of Residues	21
Details	BINDING SITE FOR RESIDUE CLA a 5558

Chain	Residue
a	CLA5560
a	PHO5561
d	LEU5182
d	CLA5354
d	MGE5361
a	PHE5119
a	TYR5147
a	PRO5150
a	SER5153
a	VAL5157
a	MET5183
a	ILE5184
a	PHE5186
a	GLN5187
a	LEU5193
a	HIS5198
a	GLY5201
a	VAL5205
a	THR5286
a	ILE5290
a	CLA5559

site_id	IC6
Number of Residues	23
Details	BINDING SITE FOR RESIDUE CLA d 5354

Chain	Residue
a	MET5183
a	PHE5206
a	CLA5558
a	CLA5559
a	CLA5560
a	PHO5562
d	VAL5152
d	VAL5156
d	PHE5181
d	LEU5182
d	PHE5185
d	GLN5186
d	TRP5191
d	THR5192
d	HIS5197
d	GLY5200
d	VAL5201
d	VAL5204
d	LEU5279
d	SER5282
d	ALA5283
d	VAL5286
d	MGE5359

site_id	IC7
Number of Residues	18
Details	BINDING SITE FOR RESIDUE CLA a 5559

Chain	Residue
a	THR5045
a	VAL5157
a	PHE5158
a	MET5172
a	ILE5176
a	THR5179
a	PHE5180
a	MET5183
a	CLA5558
c	UNL5474
d	MET5198
d	VAL5201
d	ALA5202
d	GLY5206
d	LEU5209
d	CLA5354
d	MGE5361
l	MGE5210

site_id	IC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CLA a 5560

Chain	Residue
a	GLN5199
a	VAL5202
a	ALA5203
a	GLY5207
a	LEU5210
a	TRP5278
a	CLA5558
a	PHO5562
c	DGD5509
d	PHE5157
d	VAL5175
d	PHE5179
d	LEU5182
d	CLA5354
d	MGE5359

site_id	IC9
Number of Residues	20
Details	BINDING SITE FOR RESIDUE PHO a 5561

Chain	Residue
a	LEU5041
a	ALA5044
a	THR5045
a	ILE5115
a	PHE5119
a	TYR5126
a	GLN5130
a	TYR5147
a	PRO5150
a	PHE5158
a	LEU5174
a	PRO5279
a	VAL5283
a	CLA5558
d	LEU5205
d	ALA5208
d	LEU5209
d	ILE5213
d	TRP5253
d	PHE5257

site_id	JC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE PHO a 5562

Chain	Residue
a	PHE5206
a	ALA5209
a	LEU5210
a	ALA5213
a	MET5214
a	LEU5258
a	CLA5560
d	LEU5037
d	ALA5041
d	LEU5045
d	TRP5048
d	GLY5118
d	LEU5122
d	PHE5125
d	GLN5129
d	ASN5142
d	PHE5146
d	PRO5149
d	PHE5153
d	PRO5275
d	LEU5279
d	CLA5354

site_id	JC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CLA a 5563

Chain	Residue
a	ILE5036
a	PRO5039
a	THR5040
a	PHE5093
a	PRO5095
a	ILE5096
a	TRP5097
a	LEU5114
a	PHE5117
a	HIS5118
a	LEU5121
i	TYR5009
i	THR5013
i	PHE5015
i	MGE5201

site_id	JC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CLA d 5355

Chain	Residue
c	UNL5480
d	LEU5036
d	PRO5039
d	LEU5043
d	LEU5089
d	LEU5090
d	LEU5091
d	LEU5092
d	TRP5093
d	THR5112
d	PHE5113
d	HIS5117
d	PHE5120
d	BCR5357
x	UNK5063
x	UNK5064

site_id	JC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CLA b 5511

Chain	Residue
b	TRP5185
b	PHE5190
b	CLA5512
h	PHE5041
h	BCR5107

site_id	JC5
Number of Residues	20
Details	BINDING SITE FOR RESIDUE CLA b 5512

Chain	Residue
b	GLY5189
b	PHE5190
b	GLY5197
b	ALA5200
b	HIS5201
b	ALA5204
b	ALA5205
b	VAL5208
b	PHE5247
b	PHE5250
b	CLA5511
b	CLA5513
b	CLA5518
d	LEU5158
d	ILE5159
h	PHE5038
h	PHE5041
h	ILE5045
h	LEU5046
h	TYR5049

site_id	JC6
Number of Residues	19
Details	BINDING SITE FOR RESIDUE CLA b 5513

Chain	Residue
b	ARG5068
b	LEU5069
b	ALA5146
b	LEU5149
b	CYS5150
b	PHE5153
b	LEU5158
b	HIS5201
b	HIS5202
b	PHE5247
b	VAL5252
b	THR5262
b	CLA5512
b	CLA5514
b	CLA5515
b	CLA5516
b	CLA5520
h	PHE5038
h	LEU5039

site_id	JC7
Number of Residues	19
Details	BINDING SITE FOR RESIDUE CLA b 5514

Chain	Residue
b	TRP5033
b	PHE5061
b	PHE5065
b	ARG5068
b	LEU5148
b	VAL5245
b	ALA5248
b	ALA5249
b	VAL5252
b	PHE5451
b	HIS5455
b	PHE5458
b	PHE5462
b	CLA5513
b	CLA5515
b	CLA5517
b	CLA5522
b	CLA5523
b	CLA5525

site_id	JC8
Number of Residues	17
Details	BINDING SITE FOR RESIDUE CLA b 5515

Chain	Residue
b	THR5027
b	VAL5030
b	ALA5031
b	TRP5033
b	ALA5034
b	VAL5062
b	PHE5065
b	MET5066
b	ARG5068
b	LEU5069
b	HIS5100
b	GLY5147
b	ALA5205
b	CLA5513
b	CLA5514
b	CLA5516
b	CLA5520

site_id	JC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CLA b 5516

Chain	Residue
b	LEU5069
b	GLY5070
b	TRP5091
b	ALA5099
b	HIS5100
b	LEU5103
b	GLY5152
b	PHE5153
b	PHE5156
b	HIS5157
b	PHE5162
b	GLY5163
b	PRO5164
b	CLA5513
b	CLA5515
b	BCR5529

site_id	KC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE CLA b 5517

Chain	Residue
T	BCR5104
b	TRP5033
b	TYR5040
b	GLN5058
b	GLY5059
b	PHE5061
b	LEU5324
b	PHE5325
b	THR5327
b	GLY5328
b	PRO5329
b	TRP5450
b	PHE5451
b	HIS5455
b	CLA5514
b	MGE5530
d	PHE5196
d	MET5281
l	LEU5027
m	PHE5014

site_id	KC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE CLA b 5518

Chain	Residue
b	THR5236
b	SER5239
b	ALA5243
b	PHE5246
b	PHE5463
b	HIS5466
b	LEU5474
b	CLA5512
b	CLA5519
b	CLA5520
c	UNL5481
c	UNL5482
d	ILE5123
d	MET5126
d	LEU5127
d	PHE5130
h	LEU5043
h	LEU5046

site_id	KC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CLA b 5519

Chain	Residue
b	PHE5139
b	ALA5212
b	PHE5215
b	HIS5216
b	PRO5221
b	LEU5229
b	CLA5518
b	CLA5520
h	THR5027
h	THR5028
h	MET5031
h	PHE5034
h	BCR5107

site_id	KC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CLA b 5520

Chain	Residue
b	LEU5135
b	PRO5136
b	PHE5139
b	HIS5142
b	MET5231
b	VAL5237
b	SER5240
b	CLA5513
b	CLA5515
b	CLA5518
b	CLA5519
b	CLA5522
b	CLA5525

site_id	KC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE CLA b 5521

Chain	Residue
b	TRP5005
b	TYR5006
b	ARG5007
b	VAL5008
b	HIS5009
b	LEU5238
b	ILE5242
b	LEU5461
b	PHE5462
b	PHE5464
b	GLY5465
b	TRP5468
b	HIS5469
b	ARG5472
b	PHE5479
b	CLA5522
b	CLA5523
b	CLA5524
d	MGE5360

site_id	KC6
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CLA b 5522

Chain	Residue
b	HIS5009
b	LEU5012
b	LEU5019
b	ALA5022
b	HIS5023
b	HIS5026
b	THR5027
b	VAL5237
b	LEU5238
b	SER5241
b	VAL5245
b	CLA5514
b	CLA5520
b	CLA5521
b	CLA5523
b	CLA5525

site_id	KC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CLA b 5523

Chain	Residue
b	HIS5009
b	HIS5026
b	VAL5030
b	PHE5462
b	CLA5514
b	CLA5521
b	CLA5522
b	CLA5524
b	BCR5527
b	BCR5528
d	MGE5360

site_id	KC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CLA b 5524

Chain	Residue
C	UNL475
C	UNL476
b	VAL5008
b	HIS5009
b	LEU5012
b	ALA5022
b	LEU5029
b	TRP5115
b	CLA5521
b	CLA5523
b	BCR5527
l	ARG5007
l	VAL5010
l	MGE5210
m	PHE5021

site_id	KC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CLA b 5525

Chain	Residue
b	ILE5020
b	HIS5023
b	MET5138
b	ILE5141
b	HIS5142
b	LEU5145
b	CLA5514
b	CLA5520
b	CLA5522
b	CLA5526
h	LEU5014

site_id	LC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CLA b 5526

Chain	Residue
b	ILE5020
b	LEU5024
b	ALA5110
b	TRP5113
b	HIS5114
b	LEU5120
b	CLA5525
h	THR5005
h	LEU5007

site_id	LC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLA c 5491

Chain	Residue
c	LEU5095
c	LEU5168
c	GLY5171
c	ALA5172
c	VAL5233
c	HIS5237
c	ILE5240
c	ALA5278
c	MET5281
c	VAL5296
c	TYR5297
c	CLA5492
c	CLA5493
c	BCR5506

site_id	LC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLA c 5492

Chain	Residue
c	TRP5063
c	HIS5091
c	TRP5097
c	GLY5171
c	LYS5178
c	ALA5286
c	TYR5297
c	HIS5430
c	LEU5433
c	PHE5437
c	CLA5491
c	CLA5493
c	CLA5494
c	CLA5500

site_id	LC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CLA c 5493

Chain	Residue
c	ILE5060
c	VAL5061
c	ALA5064
c	THR5068
c	LEU5088
c	HIS5091
c	ILE5092
c	LEU5095
c	VAL5114
c	HIS5118
c	LEU5279
c	UNL5477
c	CLA5491
c	CLA5492
c	CLA5500
c	CLA5502

site_id	LC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLA c 5494

Chain	Residue
c	TRP5063
c	MET5067
c	PHE5070
c	GLY5085
c	ILE5087
c	SER5406
c	TRP5425
c	SER5429
c	HIS5430
c	UNL5478
c	CLA5492
c	CLA5500
c	DGD5508
k	PRO5026

site_id	LC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CLA c 5495

Chain	Residue
a	ILE5036
a	SER5124
a	MET5127
a	TRP5131
c	ILE5265
c	TYR5274
c	GLY5277
c	ALA5278
c	LEU5438
c	HIS5441
c	LEU5442
c	ALA5445
c	ARG5449
c	CLA5497
i	PHE5023

site_id	LC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CLA c 5496

Chain	Residue
c	LEU5165
c	ILE5243
c	GLY5247
c	TRP5250
c	HIS5251
c	PRO5256
c	PHE5257
c	TRP5259
c	PHE5264
c	CLA5497
c	BCR5506
i	LEU5024

site_id	LC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLA c 5497

Chain	Residue
c	MET5157
c	LEU5161
c	HIS5164
c	LEU5168
c	PHE5264
c	TRP5266
c	TYR5271
c	TYR5274
c	SER5275
c	LEU5279
c	MET5282
c	CLA5495
c	CLA5496
c	CLA5499

site_id	LC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CLA c 5498

Chain	Residue
a	LHG5567
c	TRP5036
c	ALA5037
c	ASN5039
c	ALA5040
c	GLU5269
c	LEU5272
c	LEU5276
c	PHE5436
c	PHE5437
c	GLY5440
c	TRP5443
c	HIS5444
c	ARG5447
c	CLA5499
c	CLA5500

site_id	MC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CLA c 5499

Chain	Residue
c	ASN5039
c	LEU5049
c	ALA5052
c	HIS5053
c	HIS5056
c	GLU5269
c	LEU5272
c	SER5275
c	CLA5497
c	CLA5498
c	CLA5500

site_id	MC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLA c 5500

Chain	Residue
c	ASN5039
c	HIS5056
c	LEU5059
c	LEU5279
c	PHE5436
c	PHE5437
c	CLA5492
c	CLA5493
c	CLA5494
c	CLA5498
c	CLA5499
k	PRO5029
k	VAL5030
k	LEU5033

site_id	MC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE CLA c 5501

Chain	Residue
c	ASP5027
c	TRP5035
c	GLY5038
c	ASN5039
c	ARG5041
c	LEU5042
c	LEU5045
c	LYS5048
c	ALA5052
c	PHE5127
c	ALA5133
c	ILE5134
c	BCR5504
k	TRP5039
k	GLN5040
x	UNK5031
z	VAL5020
z	PRO5024

site_id	MC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CLA c 5502

Chain	Residue
c	HIS5053
c	PHE5147
c	PHE5163
c	HIS5164
c	VAL5167
c	LEU5168
c	GLY5171
c	CLA5493
c	CLA5503
c	BCR5505

site_id	MC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CLA c 5503

Chain	Residue
c	LEU5050
c	VAL5124
c	GLY5128
c	TYR5131
c	HIS5132
c	PRO5137
c	LEU5140
c	PHE5147
c	CLA5502
c	BCR5505

site_id	MC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEM f 5051

Chain	Residue
e	ILE5013
e	ARG5018
e	TYR5019
e	HIS5023
e	THR5026
e	ILE5027
f	ARG5019
f	TRP5020
f	HIS5024
f	ALA5027
f	ILE5031
x	UNK5116

site_id	MC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEM v 5552

Chain	Residue
v	ALA5062
v	CYS5063
v	CYS5066
v	HIS5067
v	THR5074
v	LEU5078
v	ASP5079
v	LEU5080
v	THR5084
v	TYR5101
v	TYR5108
v	HIS5118

site_id	MC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PQ9 d 5356

Chain	Residue
c	UNL5474
d	LEU5209
d	LEU5210
d	HIS5214
d	THR5217
d	TRP5253
d	ALA5260
d	PHE5261
d	LEU5267
d	PHE5270
d	VAL5274
d	THR5277

site_id	MC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PQ9 a 5564

Chain	Residue
a	HIS5215
a	LEU5218
a	ALA5251
a	HIS5252
a	PHE5255
a	SER5264
a	PHE5265
a	LEU5271
a	PHE5274

site_id	NC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE OEC a 5565

Chain	Residue
a	ASP5170
a	GLU5189
a	HIS5332
a	GLU5333
a	ASP5342
a	ALA5344
c	GLU5354

site_id	NC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BCR a 5566

Chain	Residue
a	ILE5038
a	ALA5043
a	ALA5051
a	ALA5054
a	TRP5105
i	PHE5015

site_id	NC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BCR b 5527

Chain	Residue
T	PHE19
T	BCR5104
b	MET5025
b	LEU5029
b	TRP5115
b	CLA5523
b	CLA5524
b	BCR5528
b	MGE5530

site_id	NC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE BCR T 5104

Chain	Residue
A	SQD5212
T	ILE4
T	PHE8
T	ALA11
T	ALA15
T	PHE17
T	PHE18
T	ILE21
T	PHE22
b	TRP5033
b	SER5036
b	MET5037
b	LEU5109
b	CLA5517
b	BCR5527
b	BCR5528

site_id	NC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE BCR b 5528

Chain	Residue
T	LMT217
T	BCR5104
b	LEU5029
b	GLY5032
b	TRP5033
b	SER5036
b	ILE5101
b	VAL5102
b	CLA5523
b	BCR5527

site_id	NC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BCR b 5529

Chain	Residue
A	SQD5212
T	PHE18
T	PHE22
b	LEU5106
b	CYS5112
b	VAL5116
b	TYR5117
b	CLA5516

site_id	NC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BCR h 5107

Chain	Residue
b	CLA5511
b	CLA5519
h	PHE5038
h	PHE5041
x	UNK5052
x	UNK5057

site_id	NC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE BCR d 5357

Chain	Residue
d	TYR5042
d	LEU5043
d	GLY5046
d	GLY5047
d	LEU5049
d	THR5050
d	PHE5101
d	PHE5113
d	CLA5355
f	PRO5029
f	THR5030
f	PHE5033
f	ILE5037
j	VAL5021
j	VAL5025

site_id	NC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE BCR x 5130

Chain	Residue
c	BCR5504
j	ALA5014
j	THR5015
j	GLY5018
j	MET5019
k	LEU5021
k	LEU5031
k	ALA5034
k	PHE5037
k	VAL5038
x	UNK5013
x	UNK5014
x	UNK5017
z	VAL5013

site_id	OC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE BCR c 5504

Chain	Residue
c	ALA5055
c	GLY5058
c	LEU5059
c	VAL5116
c	LEU5119
c	SER5122
c	ALA5123
c	CLA5501
c	BCR5505
k	TYR5015
k	PHE5018
k	PHE5032
k	ALA5036
x	BCR5130

site_id	OC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE BCR c 5505

Chain	Residue
c	PHE5112
c	VAL5116
c	ILE5120
c	SER5121
c	VAL5124
c	LEU5125
c	CLA5502
c	CLA5503
c	BCR5504
k	TYR5015
z	GLY5055

site_id	OC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE BCR c 5506

Chain	Residue
c	ILE5209
c	TYR5212
c	ILE5224
c	VAL5227
c	ASP5232
c	HIS5237
c	PHE5264
c	CLA5491
c	CLA5496
i	VAL5020
i	PHE5023
i	LEU5024

site_id	OC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE MGE i 5201

Chain	Residue
a	PHE5093
a	TRP5097
a	LEU5121
a	CLA5563
c	SER5216
c	PHE5218
c	TRP5223
c	MET5281
c	PHE5284
i	LYS5005
i	TYR5009

site_id	OC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE DGD c 5507

Chain	Residue
a	PHE5155
a	ILE5160
a	ILE5163
c	PRO5217
c	PHE5218
c	GLY5219
c	GLY5220
c	GLY5222
c	VAL5225
c	SER5226
c	ASN5228
c	PHE5284
c	CYS5288
c	PHE5292
c	ASN5294
c	ARG5362
c	LEU5438

site_id	OC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE LHG a 5567

Chain	Residue
a	ARG5140
a	TRP5142
a	PHE5273
c	TRP5036
c	PHE5436
c	TRP5443
c	ARG5447
c	CLA5498
d	GLU5219
d	ASN5220
d	ALA5229
d	SER5230
d	THR5231
d	PHE5232
d	SQD5358

site_id	OC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SQD d 5358

Chain	Residue
a	ASN5267
a	SER5270
a	PHE5274
a	LHG5567
c	GLU5029
c	TRP5036
d	SER5230
d	PHE5232
d	ARG5233

site_id	OC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE DGD c 5508

Chain	Residue
a	PHE5197
c	GLU5083
c	GLN5084
c	GLY5085
c	SER5406
c	ASN5418
c	PHE5419
c	VAL5420
c	TRP5425
c	THR5428
c	UNL5479
c	CLA5494
c	DGD5509
j	TYR5033

site_id	OC9
Number of Residues	20
Details	BINDING SITE FOR RESIDUE DGD c 5509

Chain	Residue
a	GLN5199
a	LEU5200
a	PHE5300
a	ASN5301
a	SER5305
a	CLA5560
c	ASN5405
c	VAL5407
c	ASN5415
c	SER5416
c	ASN5418
c	DGD5508
d	MGE5359
j	PHE5029
j	ALA5032
j	TYR5033
j	GLY5037
j	SER5038
j	SER5039
v	GLN5060

site_id	PC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE MGE d 5359

Chain	Residue
a	CLA5560
c	DGD5509
d	TYR5067
d	GLY5070
d	CYS5071
d	PHE5073
d	CLA5354
f	THR5030
f	GLN5041
j	GLY5031
j	ALA5032
j	GLY5037

site_id	PC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE DGD h 5208

Chain	Residue
b	TYR5193
b	PHE5250
b	TYR5258
b	TYR5273
b	SER5277
b	PHE5463
d	HIS5087
d	ILE5123
d	LEU5162
d	SER5165
h	TYR5049
h	VAL5060
h	SER5061
h	TRP5062

site_id	PC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE MGE d 5360

Chain	Residue
b	TRP5005
b	TYR5006
b	ARG5007
b	PHE5464
b	TRP5468
b	CLA5521
b	CLA5523
d	ARG5139
d	TYR5141
d	PHE5269
d	PHE5273
l	MGE5210

site_id	PC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE MGE l 5210

Chain	Residue
a	SER5232
a	ASN5234
a	CLA5559
b	TRP5005
b	TYR5006
b	CLA5524
c	UNL5474
d	TRP5266
d	PHE5270
d	PHE5273
d	MGE5360
l	GLU5011
l	SER5016
l	GLY5020

site_id	PC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE MGE d 5361

Chain	Residue
a	CLA5558
a	CLA5559
d	ILE5259
d	ALA5260
d	PHE5261
d	SER5262
d	ASN5263
d	TRP5266
d	PHE5270
l	ASN5013
l	THR5015
l	TYR5018
l	LEU5019
t	PHE5010
t	PHE5017
t	ALA5020

site_id	PC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SQD A 5212

Chain	Residue
A	TRP20
A	ASN26
A	ARG27
A	LEU28
T	BCR5104
b	TRP5113
b	TYR5117
b	BCR5529

site_id	PC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SQD L 5213

Chain	Residue
L	ARG14
L	TYR18
L	LEU21
T	PHE19
T	PHE23
b	ARG5018
b	LEU5029
b	SER5104

site_id	PC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE MGE b 5530

Chain	Residue
b	THR5327
b	GLY5328
b	PRO5329
b	LYS5332
b	PHE5453
b	CLA5517
b	BCR5527
l	PHE5035
m	LMT216
m	ASN5004
m	LEU5006

site_id	PC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE LMT a 5568

Chain	Residue
B	ALA43
B	LEU98
a	ILE5050
a	LEU5072
a	TYR5073
c	UNL5488
c	UNL5489
d	ARG5304
o	GLY5139
o	GLU5140
t	LMT5217

site_id	QC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE LMT M 5216

Chain	Residue
B	TYR40
B	MGE530
M	GLN5
M	LEU6
m	LMT216
m	MET5001
t	MET5001
t	ILE5004
t	LMT5217

site_id	QC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE LMT t 5217

Chain	Residue
B	TYR40
B	ALA43
B	THR44
M	LMT5216
a	LEU5072
a	LMT5568
t	MET5001
t	ILE5004

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. ItSVRYwvIHSITIP

Chain	Residue	Details
E	ILE14-PRO28
F	ILE15-PRO29

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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"}]}

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	2
Details	Site: {"description":"Tyrosine radical intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
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_FI10
Number of Residues	162
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	258
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	452
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	92
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
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_FI15
Number of Residues	586
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_FI16
Number of Residues	430
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_FI17
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_FI18
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_FI19
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_FI20
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_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":"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_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":"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_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":"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_FI24
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_FI25
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_FI26
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_FI27
Number of Residues	8
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_FI28
Number of Residues	28
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	26
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
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_FI31
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_FI32
Number of Residues	6
Details	Topological domain: {"description":"Lumenal"}

Chain

Residue

Details

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