Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1IZL

Crystal Structure of Photosystem II

Functional Information from GO Data

Chain	GOid	namespace	contents
0	0005506	molecular_function	iron ion binding
0	0009055	molecular_function	electron transfer activity
0	0009523	cellular_component	photosystem II
0	0015979	biological_process	photosynthesis
0	0019684	biological_process	photosynthesis, light reaction
0	0020037	molecular_function	heme binding
0	0022904	biological_process	respiratory electron transport chain
0	0031676	cellular_component	plasma membrane-derived thylakoid membrane
0	0042651	cellular_component	thylakoid membrane
0	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	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
J	0005506	molecular_function	iron ion binding
J	0009055	molecular_function	electron transfer activity
J	0009523	cellular_component	photosystem II
J	0009635	biological_process	response to herbicide
J	0009772	biological_process	photosynthetic electron transport in photosystem II
J	0010242	molecular_function	oxygen evolving activity
J	0015979	biological_process	photosynthesis
J	0016168	molecular_function	chlorophyll binding
J	0016491	molecular_function	oxidoreductase activity
J	0016682	molecular_function	oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor
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	0009523	cellular_component	photosystem II
K	0009539	cellular_component	photosystem II reaction center
K	0015979	biological_process	photosynthesis
L	0009521	cellular_component	photosystem
L	0009523	cellular_component	photosystem II
L	0009767	biological_process	photosynthetic electron transport chain
L	0015979	biological_process	photosynthesis
L	0016020	cellular_component	membrane
L	0016168	molecular_function	chlorophyll binding
L	0019684	biological_process	photosynthesis, light reaction
L	0031676	cellular_component	plasma membrane-derived thylakoid membrane
L	0042651	cellular_component	thylakoid membrane
M	0005737	cellular_component	cytoplasm
M	0009521	cellular_component	photosystem
M	0009523	cellular_component	photosystem II
M	0009767	biological_process	photosynthetic electron transport chain
M	0009772	biological_process	photosynthetic electron transport in photosystem II
M	0015979	biological_process	photosynthesis
M	0016020	cellular_component	membrane
M	0016168	molecular_function	chlorophyll binding
M	0019684	biological_process	photosynthesis, light reaction
M	0031676	cellular_component	plasma membrane-derived thylakoid membrane
M	0042651	cellular_component	thylakoid membrane
M	0046872	molecular_function	metal ion binding
N	0005506	molecular_function	iron ion binding
N	0005737	cellular_component	cytoplasm
N	0009055	molecular_function	electron transfer activity
N	0009523	cellular_component	photosystem II
N	0009772	biological_process	photosynthetic electron transport in photosystem II
N	0010242	molecular_function	oxygen evolving activity
N	0015979	biological_process	photosynthesis
N	0016020	cellular_component	membrane
N	0016168	molecular_function	chlorophyll binding
N	0016491	molecular_function	oxidoreductase activity
N	0019684	biological_process	photosynthesis, light reaction
N	0031676	cellular_component	plasma membrane-derived thylakoid membrane
N	0042651	cellular_component	thylakoid membrane
N	0046872	molecular_function	metal ion binding
P	0005506	molecular_function	iron ion binding
P	0005737	cellular_component	cytoplasm
P	0009055	molecular_function	electron transfer activity
P	0009523	cellular_component	photosystem II
P	0009539	cellular_component	photosystem II reaction center
P	0009767	biological_process	photosynthetic electron transport chain
P	0015979	biological_process	photosynthesis
P	0016020	cellular_component	membrane
P	0019684	biological_process	photosynthesis, light reaction
P	0020037	molecular_function	heme binding
P	0031676	cellular_component	plasma membrane-derived thylakoid membrane
P	0042651	cellular_component	thylakoid membrane
P	0046872	molecular_function	metal ion binding
Q	0005506	molecular_function	iron ion binding
Q	0005737	cellular_component	cytoplasm
Q	0009055	molecular_function	electron transfer activity
Q	0009523	cellular_component	photosystem II
Q	0009539	cellular_component	photosystem II reaction center
Q	0009767	biological_process	photosynthetic electron transport chain
Q	0015979	biological_process	photosynthesis
Q	0016020	cellular_component	membrane
Q	0019684	biological_process	photosynthesis, light reaction
Q	0020037	molecular_function	heme binding
Q	0031676	cellular_component	plasma membrane-derived thylakoid membrane
Q	0042651	cellular_component	thylakoid membrane
Q	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
W	0009523	cellular_component	photosystem II
W	0009539	cellular_component	photosystem II reaction center
W	0015979	biological_process	photosynthesis

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN A 361

Chain	Residue
A	ALA344
A	MN362
A	MN364

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN A 362

Chain	Residue
A	GLU333
A	MN361
A	MN363
A	MN364

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MN A 363

Chain	Residue
A	ASP170
A	MN362

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN A 364

Chain	Residue
A	GLU333
A	ALA344
A	MN361
A	MN362

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE FE D 353

Chain	Residue
D	HIS214

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN J 361

Chain	Residue
J	ALA344
J	MN362
J	MN364

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN J 362

Chain	Residue
J	GLU333
J	MN361
J	MN363
J	MN364

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MN J 363

Chain	Residue
J	ASP170
J	MN362

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN J 364

Chain	Residue
J	GLU189
J	ALA344
J	MN361
J	MN362

site_id	BC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE FE N 353

Chain	Residue
N	HIS214

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CLA A 365

Chain	Residue
A	PHE182
A	MET183
A	PHE186
D	CLA354

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA D 354

Chain	Residue
A	CLA365
A	CLA366
D	PHE184
D	PHE188
D	GLY200
D	VAL201

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CLA A 366

Chain	Residue
A	PHE158
D	VAL201
D	CLA354
D	PHO356

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CLA D 355

Chain	Residue
A	VAL202
A	PHO367
D	PHE173

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PHO D 356

Chain	Residue
A	TYR147
A	CLA366
D	ALA208
D	LEU209
D	ALA212

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PHO A 367

Chain	Residue
A	LEU210
D	ILE144
D	ALA145
D	ALA148
D	CLA355

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CLA A 368

Chain	Residue
A	PRO39
A	HIS92
A	TYR94
A	PRO95
A	LEU114

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CLA D 357

Chain	Residue
D	PHE113
H	UNK17

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CLA C 1078

Chain	Residue
C	GLY247
C	GLY248
C	TRP266
C	CLA1089

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CLA C 1079

Chain	Residue
C	TRP425
C	LEU426
C	SER429
C	CLA1080
K	ASP14

site_id	CC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CLA C 1080

Chain	Residue
C	HIS56
C	ILE60
C	CLA1079
C	CLA1082
C	CLA1087
K	PRO17
K	PRO20
K	VAL21

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CLA C 1081

Chain	Residue
A	SER124
A	CLA369
C	PHE264
C	TYR274

site_id	CC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CLA C 1082

Chain	Residue
C	ALA52
C	HIS56
C	GLY268
C	TYR271
C	LEU272
C	SER275
C	CLA1080
C	CLA1089

site_id	CC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CLA C 1083

Chain	Residue
C	ALA172
C	HIS237

site_id	CC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CLA C 1084

Chain	Residue
C	ILE87

site_id	CC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CLA C 1085

Chain	Residue
C	MET282
C	GLY283
C	ALA286

site_id	CC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CLA C 1086

Chain	Residue
C	HIS53
C	PHE163
C	HIS164
C	VAL167
C	CLA1088
C	LEU49
C	LEU50

site_id	DC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CLA C 1087

Chain	Residue
C	PHE436
C	PHE437
C	GLY440
C	CLA1080

site_id	DC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CLA C 1088

Chain	Residue
C	GLY128
C	GLY129
C	TYR131
C	CLA1086

site_id	DC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CLA A 369

Chain	Residue
C	CLA1081

site_id	DC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CLA C 1089

Chain	Residue
C	GLY162
C	TRP266
C	TYR271
C	TYR274
C	SER275
C	ALA278
C	LEU279
C	CLA1078
C	CLA1082

site_id	DC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CLA B 1107

Chain	Residue
B	ALA212
B	CLA1120

site_id	DC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CLA B 1108

Chain	Residue
B	VAL30
B	CLA1109
B	CLA1112
B	CLA1116
B	CLA1119

site_id	DC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA B 1109

Chain	Residue
B	ALA22
B	HIS26
B	LEU238
B	SER241
B	CLA1108
B	CLA1120

site_id	DC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CLA B 1110

Chain	Residue
B	MET60
B	TRP450
B	UNK1050

site_id	DC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA B 1111

Chain	Residue
B	ARG68
B	LEU69
B	GLY152
B	ALA155
B	CLA1113
B	CLA1114

site_id	EC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CLA B 1112

Chain	Residue
B	ALA248
B	CLA1108

site_id	EC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA B 1113

Chain	Residue
B	ALA146
B	LEU149
B	CYS150
B	TYR193
B	HIS201
B	CLA1111

site_id	EC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CLA B 1114

Chain	Residue
B	ALA31
B	PHE61
B	PRO64
B	PHE65
B	CLA1111

site_id	EC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CLA B 1116

Chain	Residue
B	HIS9
B	CLA1108

site_id	EC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CLA B 1117

Chain	Residue
B	VAL198
B	ALA200
B	ALA204

site_id	EC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA B 1118

Chain	Residue
B	LEU19
B	ILE20
B	HIS23
B	MET138
B	ILE141
B	LEU145

site_id	EC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CLA B 1119

Chain	Residue
B	HIS9
B	THR10
B	PHE464
B	GLY465
B	HIS466
B	TRP468
B	CLA1108

site_id	EC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA B 1120

Chain	Residue
B	PRO136
B	PHE139
B	SER240
B	ALA244
B	CLA1107
B	CLA1109

site_id	EC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CLA B 1121

Chain	Residue
B	ALA110

site_id	FC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE HEM E 84

Chain	Residue
E	ILE26

site_id	FC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE HEM V 138

Chain	Residue
V	PHE33
V	CYS37
V	CYS40
V	HIS41
V	HIS92

site_id	FC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PLA D 358

Chain	Residue
D	ILE213
D	HIS214
D	THR217
D	PHE257
D	LYS264

site_id	FC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE BCR K 47

Chain	Residue
D	BCR359

site_id	FC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE BCR D 359

Chain	Residue
D	TRP48
K	BCR47

site_id	FC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CLA J 365

Chain	Residue
J	PHE182
J	MET183
J	PHE186
J	PHE206
N	CLA354

site_id	FC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CLA N 354

Chain	Residue
J	CLA365
N	PHE184
N	PHE188
N	GLY200

site_id	FC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CLA N 355

Chain	Residue
J	PHE158
N	MET198
N	VAL201
N	PHO357

site_id	FC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CLA N 356

Chain	Residue
J	PHO366
N	PHE173

site_id	GC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PHO N 357

Chain	Residue
J	TYR147
N	LEU205
N	ALA208
N	LEU209
N	ALA212
N	ILE213
N	CLA355

site_id	GC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PHO J 366

Chain	Residue
J	LEU210
J	ALA213
J	MET214
N	ALA148
N	CLA356

site_id	GC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CLA J 367

Chain	Residue
J	PRO39
J	TYR94
J	PRO95
J	LEU114
J	HIS118

site_id	GC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CLA N 358

Chain	Residue
N	PRO39
N	HIS117

site_id	GC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CLA M 1078

Chain	Residue
M	GLY247
M	GLY248
M	THR255
M	CLA1088

site_id	GC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA M 1079

Chain	Residue
M	TRP425
M	LEU426
M	SER429
M	CLA1084
W	ASP14
W	CLA64

site_id	GC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CLA W 64

Chain	Residue
M	ILE60
M	CLA1079
M	CLA1081
M	CLA1084
M	CLA1086
W	PRO17
W	PRO20
W	VAL21

site_id	GC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CLA M 1080

Chain	Residue
J	SER124
J	CLA368
M	TYR274
M	GLY277

site_id	GC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CLA M 1081

Chain	Residue
M	ALA52
M	HIS56
M	LEU272
M	SER275
M	CLA1086
M	CLA1088
W	CLA64

site_id	HC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CLA M 1082

Chain	Residue
M	ALA172
M	HIS237

site_id	HC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CLA M 1084

Chain	Residue
M	LEU279
M	ALA286
M	CLA1079
W	CLA64

site_id	HC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CLA M 1085

Chain	Residue
M	HIS53
M	PHE163
M	HIS164
M	VAL167

site_id	HC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CLA M 1086

Chain	Residue
M	PHE436
M	PHE437
M	GLY440
M	CLA1081
W	CLA64

site_id	HC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CLA M 1087

Chain	Residue
M	LEU125
M	GLY128
M	GLY129
M	VAL130
M	TYR131

site_id	HC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CLA J 368

Chain	Residue
M	CLA1080

site_id	HC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CLA M 1088

Chain	Residue
M	HIS164
M	TYR271
M	TYR274
M	SER275
M	ALA278
M	LEU279
M	CLA1078
M	CLA1081

site_id	HC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CLA L 1107

Chain	Residue
L	ALA212

site_id	HC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CLA L 1108

Chain	Residue
L	VAL30
L	CLA1109
L	CLA1112
L	CLA1116
L	CLA1119

site_id	IC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CLA L 1109

Chain	Residue
L	ALA22
L	HIS26
L	LEU238
L	SER241
L	CLA1108

site_id	IC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CLA L 1110

Chain	Residue
L	MET60
L	TRP450

site_id	IC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA L 1111

Chain	Residue
L	ARG68
L	LEU69
L	GLY152
L	ALA155
L	CLA1113
L	CLA1114

site_id	IC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CLA L 1112

Chain	Residue
L	ALA248
L	CLA1108

site_id	IC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA L 1113

Chain	Residue
L	ALA146
L	LEU149
L	CYS150
L	TYR193
L	HIS201
L	CLA1111

site_id	IC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CLA L 1114

Chain	Residue
L	ALA31
L	PHE61
L	PRO64
L	PHE65
L	CLA1111

site_id	IC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CLA L 1115

Chain	Residue
L	ALA243
L	CLA1120

site_id	IC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CLA L 1116

Chain	Residue
L	CLA1108

site_id	IC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CLA L 1117

Chain	Residue
L	VAL198
L	ALA200
L	ALA204

site_id	JC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA L 1118

Chain	Residue
L	LEU19
L	ILE20
L	HIS23
L	MET138
L	ILE141
L	LEU145

site_id	JC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CLA L 1119

Chain	Residue
L	HIS9
L	PHE464
L	GLY465
L	TRP468
L	CLA1108

site_id	JC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA L 1120

Chain	Residue
L	PRO136
L	PHE139
L	HIS142
L	SER240
L	ALA244
L	CLA1115

site_id	JC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CLA L 1121

Chain	Residue
L	ALA110
L	HIS114

site_id	JC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE HEM P 92

Chain	Residue
P	ILE26

site_id	JC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE HEM 0 138

Chain	Residue
0	PHE33
0	CYS37
0	CYS40
0	HIS41
0	HIS92

site_id	JC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PLA N 359

Chain	Residue
N	ILE213
N	HIS214
N	THR217
N	PHE257
N	LYS264

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. ItSVRYwvIHSITIP

Chain	Residue	Details
E	ILE13-PRO27
F	ILE14-PRO28

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	128
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	14
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	78
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19433803","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19433803","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19433803","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12518057","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"19433803","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19433803","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19433803","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Site: {"description":"Tyrosine radical intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12518057","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

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

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	73
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_FI15
Number of Residues	208
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_FI16
Number of Residues	66
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	39
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	28
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	254
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_FI20
Number of Residues	16
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	126
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_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":"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":"14764885","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":"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_FI25
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_FI26
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"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	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_FI28
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_FI29
Number of Residues	1
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_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":"covalent","evidences":[{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12518057","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"19433803","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

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