Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1W5C

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
B	0009521	cellular_component	photosystem
B	0009523	cellular_component	photosystem II
B	0009767	biological_process	photosynthetic electron transport chain
B	0009772	biological_process	photosynthetic electron transport in photosystem II
B	0015979	biological_process	photosynthesis
B	0016020	cellular_component	membrane
B	0016168	molecular_function	chlorophyll binding
B	0019684	biological_process	photosynthesis, light reaction
B	0031676	cellular_component	plasma membrane-derived thylakoid membrane
B	0042651	cellular_component	thylakoid membrane
C	0005737	cellular_component	cytoplasm
C	0009521	cellular_component	photosystem
C	0009523	cellular_component	photosystem II
C	0009767	biological_process	photosynthetic electron transport chain
C	0009772	biological_process	photosynthetic electron transport in photosystem II
C	0015979	biological_process	photosynthesis
C	0016020	cellular_component	membrane
C	0016168	molecular_function	chlorophyll binding
C	0019684	biological_process	photosynthesis, light reaction
C	0031676	cellular_component	plasma membrane-derived thylakoid membrane
C	0042651	cellular_component	thylakoid membrane
C	0046872	molecular_function	metal ion binding
D	0005506	molecular_function	iron ion binding
D	0005737	cellular_component	cytoplasm
D	0009055	molecular_function	electron transfer activity
D	0009523	cellular_component	photosystem II
D	0009772	biological_process	photosynthetic electron transport in photosystem II
D	0010242	molecular_function	oxygen evolving activity
D	0015979	biological_process	photosynthesis
D	0016020	cellular_component	membrane
D	0016168	molecular_function	chlorophyll binding
D	0016491	molecular_function	oxidoreductase activity
D	0019684	biological_process	photosynthesis, light reaction
D	0031676	cellular_component	plasma membrane-derived thylakoid membrane
D	0042651	cellular_component	thylakoid membrane
D	0046872	molecular_function	metal ion binding
E	0005506	molecular_function	iron ion binding
E	0005737	cellular_component	cytoplasm
E	0009055	molecular_function	electron transfer activity
E	0009523	cellular_component	photosystem II
E	0009539	cellular_component	photosystem II reaction center
E	0009767	biological_process	photosynthetic electron transport chain
E	0015979	biological_process	photosynthesis
E	0016020	cellular_component	membrane
E	0019684	biological_process	photosynthesis, light reaction
E	0020037	molecular_function	heme binding
E	0031676	cellular_component	plasma membrane-derived thylakoid membrane
E	0042651	cellular_component	thylakoid membrane
E	0046872	molecular_function	metal ion binding
F	0005506	molecular_function	iron ion binding
F	0005737	cellular_component	cytoplasm
F	0009055	molecular_function	electron transfer activity
F	0009523	cellular_component	photosystem II
F	0009539	cellular_component	photosystem II reaction center
F	0009767	biological_process	photosynthetic electron transport chain
F	0015979	biological_process	photosynthesis
F	0016020	cellular_component	membrane
F	0019684	biological_process	photosynthesis, light reaction
F	0020037	molecular_function	heme binding
F	0031676	cellular_component	plasma membrane-derived thylakoid membrane
F	0042651	cellular_component	thylakoid membrane
F	0046872	molecular_function	metal ion binding
G	0005506	molecular_function	iron ion binding
G	0009055	molecular_function	electron transfer activity
G	0009523	cellular_component	photosystem II
G	0009635	biological_process	response to herbicide
G	0009772	biological_process	photosynthetic electron transport in photosystem II
G	0010242	molecular_function	oxygen evolving activity
G	0015979	biological_process	photosynthesis
G	0016168	molecular_function	chlorophyll binding
G	0016491	molecular_function	oxidoreductase activity
G	0016682	molecular_function	oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor
G	0019684	biological_process	photosynthesis, light reaction
G	0031676	cellular_component	plasma membrane-derived thylakoid membrane
G	0042651	cellular_component	thylakoid membrane
G	0046872	molecular_function	metal ion binding
H	0009521	cellular_component	photosystem
H	0009523	cellular_component	photosystem II
H	0009767	biological_process	photosynthetic electron transport chain
H	0009772	biological_process	photosynthetic electron transport in photosystem II
H	0015979	biological_process	photosynthesis
H	0016020	cellular_component	membrane
H	0016168	molecular_function	chlorophyll binding
H	0019684	biological_process	photosynthesis, light reaction
H	0031676	cellular_component	plasma membrane-derived thylakoid membrane
H	0042651	cellular_component	thylakoid membrane
I	0005737	cellular_component	cytoplasm
I	0009521	cellular_component	photosystem
I	0009523	cellular_component	photosystem II
I	0009767	biological_process	photosynthetic electron transport chain
I	0009772	biological_process	photosynthetic electron transport in photosystem II
I	0015979	biological_process	photosynthesis
I	0016020	cellular_component	membrane
I	0016168	molecular_function	chlorophyll binding
I	0019684	biological_process	photosynthesis, light reaction
I	0031676	cellular_component	plasma membrane-derived thylakoid membrane
I	0042651	cellular_component	thylakoid membrane
I	0046872	molecular_function	metal ion binding
J	0005506	molecular_function	iron ion binding
J	0005737	cellular_component	cytoplasm
J	0009055	molecular_function	electron transfer activity
J	0009523	cellular_component	photosystem II
J	0009772	biological_process	photosynthetic electron transport in photosystem II
J	0010242	molecular_function	oxygen evolving activity
J	0015979	biological_process	photosynthesis
J	0016020	cellular_component	membrane
J	0016168	molecular_function	chlorophyll binding
J	0016491	molecular_function	oxidoreductase activity
J	0019684	biological_process	photosynthesis, light reaction
J	0031676	cellular_component	plasma membrane-derived thylakoid membrane
J	0042651	cellular_component	thylakoid membrane
J	0046872	molecular_function	metal ion binding
K	0005506	molecular_function	iron ion binding
K	0005737	cellular_component	cytoplasm
K	0009055	molecular_function	electron transfer activity
K	0009523	cellular_component	photosystem II
K	0009539	cellular_component	photosystem II reaction center
K	0009767	biological_process	photosynthetic electron transport chain
K	0015979	biological_process	photosynthesis
K	0016020	cellular_component	membrane
K	0019684	biological_process	photosynthesis, light reaction
K	0020037	molecular_function	heme binding
K	0031676	cellular_component	plasma membrane-derived thylakoid membrane
K	0042651	cellular_component	thylakoid membrane
K	0046872	molecular_function	metal ion binding
L	0005506	molecular_function	iron ion binding
L	0005737	cellular_component	cytoplasm
L	0009055	molecular_function	electron transfer activity
L	0009523	cellular_component	photosystem II
L	0009539	cellular_component	photosystem II reaction center
L	0009767	biological_process	photosynthetic electron transport chain
L	0015979	biological_process	photosynthesis
L	0016020	cellular_component	membrane
L	0019684	biological_process	photosynthesis, light reaction
L	0020037	molecular_function	heme binding
L	0031676	cellular_component	plasma membrane-derived thylakoid membrane
L	0042651	cellular_component	thylakoid membrane
L	0046872	molecular_function	metal ion binding
T	0005506	molecular_function	iron ion binding
T	0009055	molecular_function	electron transfer activity
T	0009523	cellular_component	photosystem II
T	0015979	biological_process	photosynthesis
T	0020037	molecular_function	heme binding
T	0022904	biological_process	respiratory electron transport chain
T	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	0020037	molecular_function	heme binding
V	0022904	biological_process	respiratory electron transport chain
V	0042651	cellular_component	thylakoid membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE CLA A 1342

Chain	Residue
A	PHE119
A	LEU193
A	HIS198
A	GLY201
A	VAL205
A	PHE206
A	VAL283
A	THR286
A	ILE290
A	CLA1343
A	CLA1344
A	TYR147
A	PHO1345
D	LEU205
D	CLA1351
A	PRO150
A	SER153
A	MET183
A	ILE184
A	PHE186
A	GLN187
A	ILE192

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CLA A 1343

Chain	Residue
A	VAL157
A	PHE158
A	MET172
A	ILE176
A	PHE180
A	MET183
A	CLA1342
D	MET198
D	VAL201
D	ALA202
D	CLA1351

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CLA A 1344

Chain	Residue
A	GLN199
A	VAL202
A	ALA203
A	CLA1342
D	PHE157
D	VAL175
D	ILE178
D	PHE179
D	LEU182
D	CLA1351
D	PHO1352

site_id	AC4
Number of Residues	20
Details	BINDING SITE FOR RESIDUE PHO A 1345

Chain	Residue
A	LEU41
A	ALA44
A	THR45
A	ILE115
A	PHE119
A	TYR126
A	GLN130
A	ALA146
A	TYR147
A	PRO150
A	LEU174
A	GLY175
A	PRO279
A	VAL283
A	CLA1342
D	LEU205
D	ALA208
D	ALA212
D	ILE213
D	PHE257

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CLA A 1346

Chain	Residue
A	PRO39
A	THR40
A	PRO95
A	ILE96
A	TRP97
A	GLN113
A	LEU114
A	HIS118

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN A 1347

Chain	Residue
A	ASP170
A	GLU333
A	MN1349

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN A 1348

Chain	Residue
A	GLU189
A	HIS332
A	MN1349
A	MN1354

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN A 1349

Chain	Residue
A	GLU189
A	GLU333
A	MN1347
A	MN1348
A	MN1354

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 A 1350

Chain	Residue
A	HIS215
A	HIS272
D	HIS214
D	HIS268

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MN A 1354

Chain	Residue
A	MN1348
A	MN1349

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CLA B 1482

Chain	Residue
B	ASP188
B	PHE190

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CLA B 1483

Chain	Residue
B	CLA1484
B	PHE190
B	PRO192
B	ALA200
B	HIS201
B	ALA204
B	VAL208
B	PHE247

site_id	BC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLA B 1484

Chain	Residue
B	ARG68
B	LEU69
B	ALA146
B	LEU149
B	CYS150
B	PHE153
B	LEU158
B	HIS201
B	HIS202
B	VAL252
B	THR262
B	CLA1483
B	CLA1485
B	CLA1487

site_id	BC5
Number of Residues	18
Details	BINDING SITE FOR RESIDUE CLA B 1485

Chain	Residue
B	TRP33
B	PHE61
B	PHE65
B	ARG68
B	LEU69
B	VAL245
B	ALA248
B	ALA249
B	VAL252
B	PHE451
B	HIS455
B	PHE458
B	ALA459
B	CLA1484
B	CLA1486
B	CLA1488
B	CLA1492
B	CLA1494

site_id	BC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CLA B 1486

Chain	Residue
B	THR27
B	VAL30
B	ALA31
B	ALA34
B	VAL62
B	PHE65
B	MET66
B	VAL96
B	HIS100
B	CLA1485

site_id	BC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CLA B 1487

Chain	Residue
B	LEU69
B	GLY70
B	GLY152
B	PHE153
B	PHE156
B	HIS157
B	PHE162
B	PRO164
B	CLA1484

site_id	BC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CLA B 1488

Chain	Residue
B	TRP33
B	TYR40
B	GLY59
B	PHE61
B	ARG326
B	TRP450
B	PHE451
B	CLA1485
B	CLA1494
D	MET281

site_id	BC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLA B 1489

Chain	Residue
B	SER239
B	SER240
B	ALA243
B	PHE246
B	PHE247
B	PHE463
B	HIS466
B	ILE467
B	THR473
B	LEU474
B	CLA1490
D	ILE123
D	MET126
D	PHE130

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA B 1490

Chain	Residue
B	PHE139
B	PHE215
B	HIS216
B	PRO221
B	CLA1489
B	CLA1491

site_id	CC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA B 1491

Chain	Residue
B	PHE139
B	HIS142
B	VAL237
B	SER240
B	SER241
B	CLA1490

site_id	CC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CLA B 1492

Chain	Residue
B	LEU238
B	ILE242
B	LEU461
B	PHE462
B	PHE464
B	GLY465
B	TRP468
B	HIS469
B	ARG472
B	CLA1485
B	CLA1493
B	CLA1494
B	CLA1495

site_id	CC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CLA B 1493

Chain	Residue
B	LEU19
B	ALA22
B	HIS23
B	HIS26
B	GLU235
B	VAL237
B	LEU238
B	SER241
B	CLA1492
B	CLA1496

site_id	CC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CLA B 1494

Chain	Residue
B	HIS26
B	VAL30
B	PHE458
B	PHE462
B	CLA1485
B	CLA1488
B	CLA1492
B	CLA1495

site_id	CC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CLA B 1495

Chain	Residue
B	ALA22
B	LEU29
B	CLA1492
B	CLA1494

site_id	CC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CLA B 1496

Chain	Residue
B	HIS23
B	LEU24
B	LEU106
B	LEU109
B	ALA110
B	TRP113
B	MET138
B	ILE141
B	HIS142
B	LEU145
B	CLA1493
B	CLA1497

site_id	CC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA B 1497

Chain	Residue
B	LEU24
B	LEU107
B	ALA110
B	TRP113
B	HIS114
B	CLA1496

site_id	CC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CLA C 1459

Chain	Residue
C	THR94
C	LEU95
C	LEU168
C	GLY171
C	ALA172
C	VAL233
C	HIS237
C	PHE289
C	VAL296
C	TYR297
C	CLA1460

site_id	DC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CLA C 1460

Chain	Residue
C	TRP63
C	HIS91
C	GLY283
C	ALA286
C	VAL290
C	TYR297
C	HIS430
C	LEU433
C	ALA434
C	PHE437
C	CLA1459
C	CLA1462
C	CLA1468

site_id	DC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CLA C 1461

Chain	Residue
C	HIS118

site_id	DC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CLA C 1462

Chain	Residue
A	PHE300
C	TRP63
C	MET67
C	PHE70
C	GLY85
C	TRP425
C	SER429
C	CLA1460

site_id	DC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CLA C 1463

Chain	Residue
A	TRP131
C	SER273
C	TYR274
C	GLY277
C	ALA278
C	HIS441
C	LEU442
C	ALA445
C	ARG449
C	CLA1464
C	CLA1465

site_id	DC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CLA C 1464

Chain	Residue
C	ILE243
C	CYS244
C	TRP250
C	HIS251
C	PRO256
C	PHE257
C	TRP259
C	ALA260
C	PHE264
C	CLA1463
C	CLA1465

site_id	DC6
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CLA C 1465

Chain	Residue
C	MET157
C	THR158
C	LEU161
C	HIS164
C	LEU168
C	ILE240
C	PHE264
C	TRP266
C	TYR271
C	TYR274
C	SER275
C	LEU279
C	MET282
C	CLA1463
C	CLA1464
C	CLA1467

site_id	DC7
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CLA C 1466

Chain	Residue
C	TRP36
C	ALA37
C	ASN39
C	ALA40
C	LEU272
C	LEU276
C	PHE437
C	VAL439
C	GLY440
C	TRP443
C	HIS444
C	ARG447
C	CLA1467

site_id	DC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CLA C 1467

Chain	Residue
C	ASN39
C	ILE43
C	HIS53
C	HIS56
C	GLY268
C	GLU269
C	TYR271
C	LEU272
C	SER275
C	CLA1465
C	CLA1466
C	CLA1468

site_id	DC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CLA C 1468

Chain	Residue
C	HIS56
C	CLA1460
C	CLA1467

site_id	EC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA C 1469

Chain	Residue
C	ARG26
C	GLY38
C	ASN39
C	ARG41
C	LYS48
C	ALA52

site_id	EC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA C 1470

Chain	Residue
C	HIS53
C	ALA57
C	ILE160
C	PHE163
C	HIS164
C	VAL167

site_id	EC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA C 1471

Chain	Residue
C	VAL124
C	PHE127
C	GLY128
C	TYR131
C	HIS132
C	PRO137

site_id	EC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE CLA D 1351

Chain	Residue
A	MET183
A	PHE206
A	CLA1342
A	CLA1343
A	CLA1344
D	LEU122
D	VAL152
D	SER155
D	VAL156
D	LEU182
D	PHE185
D	GLN186
D	TRP191
D	HIS197
D	VAL201
D	VAL204
D	LEU279
D	PHO1352

site_id	EC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PHO D 1352

Chain	Residue
A	PHE206
A	LEU210
A	ALA213
A	MET214
A	ILE259
A	CLA1344
D	GLY118
D	PHE125
D	ASN142
D	ALA145
D	PHE146
D	PRO149
D	PHE153
D	PHE173
D	PRO275
D	LEU279
D	CLA1351

site_id	EC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CLA D 1353

Chain	Residue
D	LEU36
D	LEU43
D	LEU89
D	LEU90
D	LEU91
D	LEU92
D	TRP93
D	THR112
D	PHE113
D	HIS117

site_id	EC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PL9 D 1354

Chain	Residue
D	THR217
D	TRP253
D	PHE261
D	LEU267

site_id	EC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE HEM E 1085

Chain	Residue
E	TYR19
E	HIS23
E	THR26
F	TRP20
F	HIS24
F	ALA27

site_id	EC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BCR F 1046

Chain	Residue
D	TYR42
D	LEU49
D	PHE101
D	PHE113
F	PRO29
F	THR30
F	PHE33

site_id	FC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE CLA G 1342

Chain	Residue
G	PHE119
G	TYR147
G	PRO150
G	SER153
G	MET183
G	ILE184
G	PHE186
G	GLN187
G	ILE192
G	LEU193
G	HIS198
G	GLY201
G	VAL205
G	PHE206
G	VAL283
G	THR286
G	ILE290
G	CLA1343
G	CLA1344
G	PHO1345
J	LEU205
J	CLA1351

site_id	FC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CLA G 1343

Chain	Residue
G	VAL157
G	PHE158
G	MET172
G	ILE176
G	PHE180
G	MET183
G	CLA1342
J	MET198
J	VAL201
J	ALA202
J	LEU209
J	CLA1351

site_id	FC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CLA G 1344

Chain	Residue
G	GLN199
G	VAL202
G	ALA203
G	CLA1342
J	PHE157
J	VAL175
J	ILE178
J	PHE179
J	LEU182
J	CLA1351
J	PHO1352

site_id	FC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE PHO G 1345

Chain	Residue
G	LEU41
G	ALA44
G	THR45
G	PHE48
G	ILE115
G	PHE119
G	TYR126
G	GLN130
G	ALA146
G	TYR147
G	PRO150
G	LEU174
G	GLY175
G	PRO279
G	VAL283
G	CLA1342
J	LEU205
J	ALA208
J	ALA212
J	ILE213
J	PHE257

site_id	FC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CLA G 1346

Chain	Residue
G	PRO39
G	THR40
G	PHE93
G	PRO95
G	ILE96
G	TRP97
G	GLN113
G	LEU114
G	HIS118

site_id	FC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN G 1347

Chain	Residue
G	ASP170
G	GLU333
G	MN1349

site_id	FC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN G 1348

Chain	Residue
G	GLU189
G	HIS332
G	MN1349
G	MN5054

site_id	FC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN G 1349

Chain	Residue
G	ASP170
G	GLU189
G	GLU333
G	MN1347
G	MN1348
G	MN5054

site_id	FC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 G 1350

Chain	Residue
G	HIS215
G	HIS272
J	HIS214
J	HIS268

site_id	GC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MN G 5054

Chain	Residue
G	MN1348
G	MN1349

site_id	GC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CLA H 1482

Chain	Residue
H	ASP188
H	PHE190

site_id	GC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CLA H 1483

Chain	Residue
H	PHE190
H	PRO192
H	ALA200
H	HIS201
H	ALA204
H	VAL208
H	PHE247
H	THR255
H	CLA1484

site_id	GC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLA H 1484

Chain	Residue
H	ARG68
H	LEU69
H	ALA146
H	LEU149
H	CYS150
H	PHE153
H	MET166
H	HIS201
H	HIS202
H	VAL252
H	THR262
H	CLA1483
H	CLA1485
H	CLA1487

site_id	GC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE CLA H 1485

Chain	Residue
H	TRP33
H	PHE61
H	PHE65
H	ARG68
H	VAL245
H	ALA248
H	ALA249
H	VAL252
H	PHE451
H	HIS455
H	PHE458
H	ALA459
H	CLA1484
H	CLA1486
H	CLA1488
H	CLA1492
H	CLA1494

site_id	GC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CLA H 1486

Chain	Residue
H	THR27
H	VAL30
H	ALA31
H	ALA34
H	VAL62
H	PHE65
H	MET66
H	VAL96
H	HIS100
H	CLA1485

site_id	GC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CLA H 1487

Chain	Residue
H	LEU69
H	GLY70
H	GLY152
H	PHE153
H	PHE156
H	HIS157
H	PHE162
H	PRO164
H	CLA1484

site_id	GC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CLA H 1488

Chain	Residue
H	TRP33
H	TYR40
H	GLY59
H	PHE61
H	ARG326
H	TRP450
H	PHE451
H	CLA1485
H	CLA1494
J	MET281

site_id	GC9
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CLA H 1489

Chain	Residue
H	THR236
H	SER240
H	ALA243
H	PHE246
H	PHE247
H	PHE463
H	HIS466
H	ILE467
H	THR473
H	LEU474
H	CLA1490
J	ILE123
J	MET126
J	LEU127
J	PHE130

site_id	HC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA H 1490

Chain	Residue
H	PHE139
H	PHE215
H	HIS216
H	PRO221
H	CLA1489
H	CLA1491

site_id	HC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA H 1491

Chain	Residue
H	PHE139
H	HIS142
H	VAL237
H	SER240
H	SER241
H	CLA1490

site_id	HC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CLA H 1492

Chain	Residue
H	LEU238
H	ILE242
H	LEU461
H	PHE462
H	PHE464
H	GLY465
H	TRP468
H	HIS469
H	ARG472
H	CLA1485
H	CLA1493
H	CLA1494
H	CLA1495

site_id	HC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CLA H 1493

Chain	Residue
H	LEU19
H	ALA22
H	HIS23
H	HIS26
H	GLU235
H	VAL237
H	LEU238
H	SER241
H	CLA1492
H	CLA1496

site_id	HC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CLA H 1494

Chain	Residue
H	HIS26
H	VAL30
H	PHE458
H	PHE462
H	CLA1485
H	CLA1488
H	CLA1492
H	CLA1495

site_id	HC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CLA H 1495

Chain	Residue
H	ALA22
H	LEU29
H	CLA1492
H	CLA1494

site_id	HC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CLA H 1496

Chain	Residue
H	HIS23
H	LEU24
H	LEU106
H	LEU109
H	ALA110
H	TRP113
H	MET138
H	ILE141
H	HIS142
H	LEU145
H	CLA1493
H	CLA1497

site_id	HC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA H 1497

Chain	Residue
H	LEU24
H	LEU107
H	ALA110
H	TRP113
H	HIS114
H	CLA1496

site_id	HC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CLA I 1459

Chain	Residue
I	THR94
I	LEU95
I	LEU168
I	GLY171
I	ALA172
I	VAL233
I	HIS237
I	PHE289
I	VAL296
I	TYR297
I	CLA1460

site_id	IC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLA I 1460

Chain	Residue
I	TRP63
I	HIS91
I	GLY283
I	ALA286
I	VAL290
I	TYR297
I	HIS430
I	LEU433
I	ALA434
I	PHE437
I	CLA1459
I	CLA1461
I	CLA1462
I	CLA1468

site_id	IC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CLA I 1461

Chain	Residue
I	VAL61
I	HIS118
I	CLA1460

site_id	IC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CLA I 1462

Chain	Residue
G	PHE300
I	TRP63
I	MET67
I	PHE70
I	GLY85
I	TRP425
I	SER429
I	CLA1460

site_id	IC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CLA I 1463

Chain	Residue
G	TRP131
I	SER273
I	TYR274
I	GLY277
I	ALA278
I	HIS441
I	LEU442
I	ALA445
I	ARG449
I	CLA1464
I	CLA1465

site_id	IC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CLA I 1464

Chain	Residue
I	ILE243
I	CYS244
I	TRP250
I	HIS251
I	PRO256
I	PHE257
I	TRP259
I	ALA260
I	PHE264
I	CLA1463
I	CLA1465

site_id	IC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CLA I 1465

Chain	Residue
I	MET157
I	THR158
I	LEU161
I	HIS164
I	LEU168
I	ILE240
I	PHE264
I	TRP266
I	TYR271
I	TYR274
I	SER275
I	MET282
I	CLA1463
I	CLA1464
I	CLA1467

site_id	IC7
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CLA I 1466

Chain	Residue
I	TRP36
I	ALA37
I	ASN39
I	ALA40
I	LEU272
I	LEU276
I	PHE437
I	VAL439
I	GLY440
I	TRP443
I	HIS444
I	ARG447
I	CLA1467

site_id	IC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CLA I 1467

Chain	Residue
I	ASN39
I	ILE43
I	ALA52
I	HIS53
I	HIS56
I	GLY268
I	GLU269
I	TYR271
I	LEU272
I	SER275
I	CLA1465
I	CLA1466
I	CLA1468

site_id	IC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CLA I 1468

Chain	Residue
I	HIS56
I	CLA1460
I	CLA1467

site_id	JC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA I 1469

Chain	Residue
I	ARG26
I	GLY38
I	ASN39
I	ARG41
I	LYS48
I	ALA52

site_id	JC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA I 1470

Chain	Residue
I	HIS53
I	ALA57
I	ILE160
I	PHE163
I	HIS164
I	VAL167

site_id	JC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CLA I 1471

Chain	Residue
I	VAL124
I	PHE127
I	GLY128
I	TYR131
I	HIS132

site_id	JC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE CLA J 1351

Chain	Residue
G	MET183
G	PHE206
G	CLA1342
G	CLA1343
G	CLA1344
J	LEU122
J	VAL152
J	SER155
J	VAL156
J	LEU182
J	PHE185
J	GLN186
J	TRP191
J	HIS197
J	VAL201
J	VAL204
J	LEU279
J	PHO1352

site_id	JC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PHO J 1352

Chain	Residue
G	PHE206
G	LEU210
G	ALA213
G	MET214
G	ILE259
G	CLA1344
J	GLY118
J	PHE125
J	ASN142
J	ALA145
J	PHE146
J	PRO149
J	PHE153
J	PHE173
J	PRO275
J	LEU279
J	CLA1351

site_id	JC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CLA J 1353

Chain	Residue
J	LEU36
J	LEU43
J	LEU89
J	LEU90
J	LEU91
J	LEU92
J	TRP93
J	THR112
J	PHE113
J	HIS117

site_id	JC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PL9 J 1354

Chain	Residue
J	TRP253
J	PHE261
J	LEU267

site_id	JC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE HEM L 1046

Chain	Residue
K	TYR19
K	HIS23
K	THR26
L	TRP20
L	HIS24
L	ALA27

site_id	JC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BCR L 1047

Chain	Residue
J	TYR42
J	LEU49
J	PHE101
J	PHE113
L	PRO29
L	THR30
L	PHE33

site_id	KC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEC T 1138

Chain	Residue
T	ALA36
T	CYS37
T	CYS40
T	HIS41
T	THR48
T	LEU52
T	ASP53
T	THR58
T	LEU59
T	ALA62
T	LEU72
T	TYR75
T	MET76
T	TYR82
T	HIS92
T	ILE115

site_id	KC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEC V 1138

Chain	Residue
V	ALA36
V	CYS37
V	CYS40
V	HIS41
V	THR48
V	LEU52
V	ASP53
V	THR58
V	LEU59
V	ALA62
V	LEU72
V	TYR75
V	TYR82
V	HIS92
V	ILE115

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASN191-SER217
D	ASN190-ALA216

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

Chain	Residue	Details
F	ILE15-PRO29
E	ILE14-PRO28

Functional Information from SwissProt/UniProt

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

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	744
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	80
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	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_FI11
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_FI12
Number of Residues	210
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	452
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	70
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
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_FI16
Number of Residues	170
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_FI17
Number of Residues	302
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_FI18
Number of Residues	176
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_FI19
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_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":"14764885","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: {"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_FI22
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_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":"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_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"}]}

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":"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	28
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00642","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
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_FI28
Number of Residues	32
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00643","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	16
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
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_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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)