Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3KZI

Crystal Structure of Monomeric Form of Cyanobacterial Photosystem II

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 A 361

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

site_id	AC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE CLA A 362

Chain	Residue
A	ALA154
A	VAL157
A	PHE182
A	MET183
A	PHE186
A	GLN187
A	LEU193
A	HIS198
A	VAL205
A	THR286
A	ALA287
A	ILE290
A	CLA363
A	CLA364
A	PHO365
D	LEU182
D	CLA354
T	PHE17
A	PHE119
A	TYR147
A	PRO150
A	SER153

site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE CLA A 363

Chain	Residue
A	THR45
A	VAL157
A	PHE158
A	MET172
A	ILE176
A	THR179
A	MET183
A	CLA362
A	PHO365
D	MET198
D	VAL201
D	ALA202
D	CLA354
D	PL9357
D	LMG360
L	LEU30
T	PHE10
T	ILE14

site_id	AC4
Number of Residues	19
Details	BINDING SITE FOR RESIDUE PHO A 365

Chain	Residue
A	LEU41
A	THR45
A	PHE48
A	PHE119
A	TYR126
A	GLN130
A	TYR147
A	PRO150
A	LEU174
A	CLA362
A	CLA363
D	LEU205
D	ALA208
D	LEU209
D	ALA212
D	ILE213
D	TRP253
D	PHE257
D	LMG360

site_id	AC5
Number of Residues	18
Details	BINDING SITE FOR RESIDUE CLA A 366

Chain	Residue
A	VAL35
A	ILE36
A	PRO39
A	THR40
A	PHE93
A	ILE96
A	TRP97
A	LEU114
A	PHE117
A	HIS118
A	LEU121
A	BCR369
C	DGD474
C	CLA481
I	VAL8
I	TYR9
I	VAL12
I	PHE15

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MES A 367

Chain	Residue
A	MET214
A	HIS215
A	LEU218
A	VAL219
A	TYR246
A	ALA251
A	LEU271

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE OEC A 368

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

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE BCR A 369

Chain	Residue
A	LEU42
A	ALA43
A	ILE46
A	ALA51
A	ALA55
A	TRP105
A	LEU106
A	CLA366
A	VAL35
A	ILE38
A	PRO39

site_id	AC9
Number of Residues	18
Details	BINDING SITE FOR RESIDUE DGD C 474

Chain	Residue
A	PHE93
A	PRO95
A	TRP97
A	GLU98
A	LEU121
A	PHE155
A	CLA366
C	LEU213
C	LEU214
C	LYS215
C	SER216
C	PRO217
C	TRP223
C	MET281
C	PHE284
C	CLA481
C	DGD491
I	LYS5

site_id	BC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE LHG A 371

Chain	Residue
A	ARG140
A	TRP142
A	PHE273
C	TRP36
C	PHE436
C	TRP443
C	ARG447
C	SQD475
C	CLA480
C	CLA484
D	ALA229
D	SER230
D	THR231
D	PHE232

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SQD C 475

Chain	Residue
A	PHE273
A	LHG371
C	ALA34
C	TRP36
C	LHG476
C	CLA484
D	PHE232
D	ARG233
D	LMG359
J	BCR115

site_id	BC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE LMG A 373

Chain	Residue
A	SER232
A	ASN234
A	TYR235
B	PRO4
B	TRP5
B	TYR6
B	CLA521
D	TRP266
D	PHE273
D	PL9357
D	LMG360
L	GLU11
L	ASN13
L	SER16
L	GLY20
L	LEU23
L	ILE24
L	VAL26
M	PRO18
M	LEU22

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE LHG C 476

Chain	Residue
C	SQD475
C	DGD492
J	BCR115

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DGD A 375

Chain	Residue
A	ILE46
A	ILE50
A	LMT376
I	LMG220
I	LMT274
O	LMT274

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE LMT A 376

Chain	Residue
A	ALA54
A	ASP103
A	DGD375

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CLA B 511

Chain	Residue
B	TRP185
B	PRO187
B	PHE190
B	ALA204
B	CLA512
X	BCR107

site_id	BC8
Number of Residues	17
Details	BINDING SITE FOR RESIDUE CLA B 512

Chain	Residue
B	GLY189
B	PHE190
B	PRO192
B	HIS201
B	ALA204
B	VAL208
B	PHE247
B	PHE250
B	CLA511
B	CLA513
B	DGD528
H	PHE38
H	PHE41
H	LEU42
H	ILE45
H	TYR49
X	BCR107

site_id	BC9
Number of Residues	21
Details	BINDING SITE FOR RESIDUE CLA B 513

Chain	Residue
B	ARG68
B	LEU69
B	LEU149
B	CYS150
B	PHE153
B	MET166
B	HIS201
B	HIS202
B	PHE247
B	ALA248
B	VAL251
B	VAL252
B	THR255
B	THR262
B	CLA512
B	CLA514
B	CLA515
B	CLA516
B	CLA519
B	CLA520
H	PHE38

site_id	CC1
Number of Residues	23
Details	BINDING SITE FOR RESIDUE CLA B 514

Chain	Residue
B	TRP33
B	PHE61
B	PHE65
B	ARG68
B	LEU148
B	LEU149
B	VAL245
B	ALA248
B	ALA249
B	VAL252
B	PHE451
B	HIS455
B	PHE458
B	ALA459
B	PHE462
B	CLA513
B	CLA515
B	CLA517
B	CLA520
B	CLA521
B	CLA522
B	CLA523
B	CLA525

site_id	CC2
Number of Residues	21
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	HIS100
B	LEU103
B	GLY147
B	ALA205
B	CLA513
B	CLA514
B	CLA516
B	CLA519
B	CLA520
B	CLA522
B	BCR530

site_id	CC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CLA B 516

Chain	Residue
B	TRP91
B	VAL96
B	ALA99
B	HIS100
B	LEU103
B	LEU106
B	LEU149
B	GLY152
B	PHE153
B	PHE156
B	HIS157
B	PHE162
B	PRO164
B	CLA513
B	CLA515
B	CLA526

site_id	CC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE CLA B 517

Chain	Residue
B	TRP33
B	MET37
B	TYR40
B	GLN58
B	GLY59
B	PHE61
B	PHE325
B	ARG326
B	THR327
B	GLY328
B	PRO329
B	TRP450
B	PHE451
B	ALA454
B	CLA514
B	CLA523
B	BCR529
B	LMG531
B	DGD533
D	MET199
D	MET281
M	PHE14

site_id	CC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE CLA B 518

Chain	Residue
B	THR236
B	SER239
B	SER240
B	ALA243
B	PHE246
B	PHE247
B	HIS466
B	CLA519
B	CLA520
D	PHE120
D	ILE123
D	MET126
D	LEU127
D	PHE130
D	CLA356
D	SQD361
H	LEU43

site_id	CC6
Number of Residues	20
Details	BINDING SITE FOR RESIDUE CLA B 519

Chain	Residue
B	PHE139
B	VAL208
B	ALA212
B	PHE215
B	HIS216
B	ARG220
B	PRO221
B	PRO222
B	LEU225
B	LEU229
B	CLA513
B	CLA515
B	CLA518
B	CLA520
H	THR27
H	THR28
H	MET31
H	PHE34
H	LEU46
X	BCR107

site_id	CC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLA B 520

Chain	Residue
B	PHE139
B	HIS142
B	LEU143
B	MET231
B	ILE234
B	VAL237
B	SER240
B	CLA513
B	CLA514
B	CLA515
B	CLA518
B	CLA519
B	CLA522
B	CLA525

site_id	CC8
Number of Residues	20
Details	BINDING SITE FOR RESIDUE CLA B 521

Chain	Residue
A	LMG373
B	TRP5
B	TYR6
B	ARG7
B	HIS9
B	ILE242
B	LEU461
B	PHE462
B	PHE464
B	GLY465
B	TRP468
B	HIS469
B	ARG472
B	PHE479
B	CLA514
B	CLA522
B	CLA523
B	CLA524
B	LMG531
M	PHE21

site_id	CC9
Number of Residues	17
Details	BINDING SITE FOR RESIDUE CLA B 522

Chain	Residue
B	HIS9
B	HIS23
B	HIS26
B	THR27
B	ILE234
B	GLU235
B	VAL237
B	LEU238
B	SER241
B	ILE242
B	CLA514
B	CLA515
B	CLA520
B	CLA521
B	CLA523
B	CLA524
B	CLA525

site_id	DC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CLA B 523

Chain	Residue
B	HIS9
B	HIS26
B	VAL30
B	TRP33
B	PHE462
B	CLA514
B	CLA517
B	CLA521
B	CLA522
B	CLA524
B	BCR527
B	LMG531

site_id	DC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CLA B 524

Chain	Residue
B	VAL8
B	HIS9
B	ALA22
B	TRP115
B	CLA521
B	CLA522
B	CLA523
B	BCR527
B	DGD533
L	VAL10
M	PHE21
M	LEU25

site_id	DC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CLA B 525

Chain	Residue
B	HIS23
B	LEU24
B	MET138
B	HIS142
B	LEU145
B	CLA514
B	CLA520
B	CLA522
B	CLA526
B	BCR530
H	LEU14

site_id	DC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CLA B 526

Chain	Residue
B	LEU24
B	ALA110
B	TRP113
B	HIS114
B	CLA516
B	CLA525
B	BCR530
H	THR5
H	LEU7
H	GLY8

site_id	DC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BCR B 527

Chain	Residue
B	MET25
B	LEU29
B	ALA111
B	TRP115
B	CLA523
B	CLA524
B	BCR529
B	DGD533
M	LEU13

site_id	DC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BCR B 529

Chain	Residue
B	LEU29
B	TRP33
B	GLY105
B	CLA517
B	BCR527
B	DGD533

site_id	DC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE BCR B 530

Chain	Residue
B	CLA515
B	CLA525
B	CLA526
B	LMT535

site_id	DC8
Number of Residues	17
Details	BINDING SITE FOR RESIDUE LMG B 531

Chain	Residue
A	ALA233
B	TYR6
B	ARG7
B	PHE464
B	TRP468
B	PHE479
B	CLA517
B	CLA521
B	CLA523
B	DGD533
D	ARG139
D	TYR141
D	PHE269
D	LEU272
D	VAL276
M	PHE14
M	PRO18

site_id	DC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE DGD B 533

Chain	Residue
B	THR327
B	LYS332
B	LEU461
B	CLA517
B	CLA524
B	BCR527
B	BCR529
B	LMG531
D	ILE284
L	PHE35
M	ASN4
M	LEU6
M	ALA10
M	LEU13
M	PHE14
M	VAL17

site_id	EC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE LMT B 535

Chain	Residue
B	TRP91
B	LEU149
B	BCR530

site_id	EC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE LMT D 536

Chain	Residue
B	LYS227
D	ASP19
D	ASP20
D	LYS23
D	SQD361
H	MET35

site_id	EC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CLA C 477

Chain	Residue
C	LEU95
C	LEU168
C	GLY171
C	ALA172
C	TRP223
C	ILE224
C	HIS237
C	ILE240
C	PHE289
C	VAL296
C	TYR297
C	CLA478
C	CLA479
C	CLA482
C	CLA483
C	BCR490

site_id	EC4
Number of Residues	20
Details	BINDING SITE FOR RESIDUE CLA C 478

Chain	Residue
C	TRP63
C	HIS91
C	LEU174
C	LEU175
C	LYS178
C	PHE182
C	LEU279
C	MET282
C	GLY283
C	ALA286
C	VAL290
C	TYR297
C	HIS430
C	LEU433
C	ALA434
C	PHE437
C	CLA477
C	CLA479
C	CLA480
K	CLA483

site_id	EC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLA C 479

Chain	Residue
C	ILE60
C	VAL61
C	TRP63
C	ALA64
C	THR68
C	LEU88
C	HIS91
C	LEU95
C	VAL114
C	HIS118
C	CLA477
C	CLA478
C	LMG494
K	CLA483

site_id	EC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE CLA C 480

Chain	Residue
A	VAL281
A	LHG371
C	TRP63
C	MET67
C	PHE70
C	GLN84
C	GLY85
C	LEU404
C	TRP425
C	LEU426
C	SER429
C	CLA478
C	CLA484
C	DGD492
C	DGD493
J	LMG492
K	PRO26
K	CLA483

site_id	EC7
Number of Residues	18
Details	BINDING SITE FOR RESIDUE CLA C 481

Chain	Residue
A	PHE33
A	MET127
A	GLY128
A	TRP131
A	CLA366
C	PHE264
C	ILE265
C	TYR274
C	GLY277
C	MET281
C	HIS441
C	LEU442
C	ALA445
C	ARG449
C	DGD474
C	CLA483
C	BCR490
I	PHE23

site_id	EC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CLA C 482

Chain	Residue
C	LEU161
C	LEU165
C	ILE243
C	CYS244
C	TRP250
C	HIS251
C	THR255
C	PRO256
C	PHE257
C	TRP259
C	ALA260
C	PHE264
C	CLA477
C	CLA483
C	BCR490

site_id	EC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CLA C 483

Chain	Residue
C	MET157
C	LEU161
C	HIS164
C	LEU165
C	LEU168
C	ILE240
C	PHE264
C	TRP266
C	TYR271
C	TYR274
C	SER275
C	CLA477
C	CLA481
C	CLA482
C	CLA485
C	BCR490

site_id	FC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE CLA C 484

Chain	Residue
A	LHG371
C	TRP36
C	ALA37
C	GLY38
C	ASN39
C	ALA40
C	GLU269
C	LEU276
C	PHE436
C	PHE437
C	GLY440
C	TRP443
C	HIS444
C	ARG447
C	SQD475
C	CLA480
C	CLA485
C	CLA486
K	CLA483

site_id	FC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE CLA C 485

Chain	Residue
C	ASN39
C	ILE43
C	LEU49
C	ALA52
C	HIS53
C	HIS56
C	TRP151
C	HIS164
C	GLY268
C	TYR271
C	LEU272
C	SER275
C	LEU276
C	LEU279
C	CLA483
C	CLA484
C	CLA487
K	CLA483

site_id	FC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CLA K 483

Chain	Residue
C	HIS56
C	LEU59
C	ILE60
C	TRP63
C	LEU279
C	PHE436
C	PHE437
C	CLA478
C	CLA479
C	CLA480
C	CLA484
C	CLA485
C	CLA486
K	PRO29
K	VAL30
K	LEU33

site_id	FC4
Number of Residues	28
Details	BINDING SITE FOR RESIDUE CLA C 486

Chain	Residue
C	GLN28
C	TRP35
C	GLY38
C	ASN39
C	ARG41
C	LEU42
C	LEU45
C	LYS48
C	ALA52
C	ALA123
C	PHE127
C	VAL130
C	ALA133
C	ILE134
C	CLA484
C	BCR489
K	PHE32
K	LEU33
K	PHE37
K	TRP39
K	GLN40
K	CLA483
Z	MET19
Z	VAL20
Z	PRO24
y	ILE35
y	LEU39
y	ASN45

site_id	FC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLA C 487

Chain	Residue
C	HIS53
C	VAL54
C	ALA57
C	LEU125
C	ILE160
C	PHE163
C	HIS164
C	VAL167
C	ILE170
C	GLY171
C	LEU174
C	CLA485
C	CLA488
Z	BCR116

site_id	FC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CLA C 488

Chain	Residue
C	VAL54
C	VAL124
C	LEU125
C	GLY128
C	TYR131
C	HIS132
C	PHE147
C	CLA487
Z	BCR116

site_id	FC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE BCR C 489

Chain	Residue
C	ALA55
C	GLY58
C	LEU59
C	VAL116
C	LEU119
C	SER122
C	ALA123
C	CLA486
J	BCR112
K	TYR15
K	PHE18
K	LEU21
Z	LEU9
Z	VAL13
Z	VAL20

site_id	FC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE BCR C 490

Chain	Residue
C	ILE209
C	PHE210
C	TYR212
C	LEU213
C	VAL227
C	ASP232
C	VAL233
C	HIS237
C	ILE240
C	PHE264
C	CLA477
C	CLA481
C	CLA482
C	CLA483
I	PHE23

site_id	FC9
Number of Residues	18
Details	BINDING SITE FOR RESIDUE DGD C 491

Chain	Residue
A	PHE155
A	ILE160
C	PRO217
C	PHE218
C	GLY219
C	GLY220
C	TRP223
C	VAL225
C	PHE284
C	CYS288
C	PHE292
C	ASN293
C	ASN294
C	THR295
C	ASP360
C	ARG362
C	LEU438
C	DGD474

site_id	GC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE DGD C 492

Chain	Residue
A	PHE197
A	THR292
C	GLU83
C	GLN84
C	GLY85
C	SER406
C	ASN418
C	PHE419
C	VAL420
C	TRP425
C	VAL432
C	LHG476
C	CLA480
C	DGD493
J	PHE29
J	TYR33
J	BCR115
J	LMG492

site_id	GC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE DGD C 493

Chain	Residue
A	LEU200
A	ALA203
A	TRP278
A	VAL281
A	PHE300
A	CLA364
C	LEU404
C	ASN405
C	SER406
C	VAL407
C	ASN415
C	SER416
C	VAL417
C	ASN418
C	CLA480
C	DGD492
D	LMG359
J	PHE29
J	ALA32
J	TYR33
J	GLY37
J	SER38
J	SER39
J	LEU40

site_id	GC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE LMG J 492

Chain	Residue
C	HIS74
C	CLA480
C	DGD492
J	ILE22
J	BCR115
K	VAL30
y	ILE25

site_id	GC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE LMG C 494

Chain	Residue
C	PHE109
C	PRO110
C	VAL113
C	VAL114
C	VAL117
C	CLA479
Z	BCR116

site_id	GC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BCT D 353

Chain	Residue
A	HIS215
A	TYR246
A	HIS272
A	FE2361
D	HIS214
D	TYR244
D	LYS264
D	HIS268

site_id	GC6
Number of Residues	25
Details	BINDING SITE FOR RESIDUE CLA D 354

Chain	Residue
A	PHE206
A	CLA362
A	CLA363
A	CLA364
D	TRP48
D	LEU122
D	PRO149
D	VAL152
D	SER155
D	VAL156
D	PHE181
D	LEU182
D	PHE185
D	GLN186
D	TRP191
D	THR192
D	HIS197
D	VAL201
D	VAL204
D	LEU279
D	SER282
D	ALA283
D	VAL286
D	PHO355
D	LMG359

site_id	GC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLA A 364

Chain	Residue
A	GLN199
A	VAL202
A	ALA203
A	CLA362
C	DGD493
D	PHE153
D	PHE157
D	VAL175
D	ILE178
D	PHE181
D	LEU182
D	CLA354
D	PHO355
D	LMG359

site_id	GC8
Number of Residues	20
Details	BINDING SITE FOR RESIDUE PHO D 355

Chain	Residue
A	LEU210
A	MET214
A	ILE259
A	CLA364
D	LEU37
D	ALA41
D	ALA44
D	TRP48
D	GLY118
D	GLY121
D	LEU122
D	PHE125
D	ASN142
D	PHE146
D	ALA148
D	PRO149
D	GLY174
D	PRO275
D	LEU279
D	CLA354

site_id	GC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CLA D 356

Chain	Residue
B	CLA518
D	ILE35
D	PRO39
D	LEU43
D	LEU89
D	LEU90
D	LEU91
D	LEU92
D	TRP93
D	TRP104
D	THR112
D	PHE113
D	HIS117
H	VAL40
X	LEU23
X	GLY26

site_id	HC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PL9 D 357

Chain	Residue
A	ILE53
A	CLA363
A	LMG373
D	ALA202
D	LEU210
D	ILE213
D	HIS214
D	THR217
D	MET246
D	TRP253
D	ALA260
D	PHE261
D	LEU267
D	VAL274
D	LMG360
L	VAL26
L	LEU29
T	PHE10

site_id	HC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE BCR D 358

Chain	Residue
D	TYR42
D	GLY46
D	GLY47
D	LEU49
D	THR50
D	PHE113
D	LMG359
F	PRO29
F	PHE33
F	LEU34
J	VAL21
J	VAL25

site_id	HC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE LMG D 359

Chain	Residue
A	CLA364
C	SQD475
C	DGD493
D	TYR67
D	CYS71
D	CLA354
D	BCR358
F	LEU26
F	ILE37
F	MET40
F	GLN41
J	PHE28
J	GLY31
J	ALA32
J	GLY37

site_id	HC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE LMG D 360

Chain	Residue
A	CLA363
A	PHO365
A	LMG373
D	ILE259
D	ALA260
D	PHE261
D	SER262
D	ASN263
D	TRP266
D	PL9357
L	THR15
L	LEU19
L	LEU22
T	PHE10
T	ILE13
T	PHE17
T	ALA20
T	ILE21

site_id	HC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SQD D 361

Chain	Residue
B	LYS227
B	ARG230
B	CLA518
D	LYS23
D	TRP32
D	ARG134
D	LEU135
D	LMT536
X	PHE34

site_id	HC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DGD D 362

Chain	Residue
D	PHE101
D	ARG103
F	SQD224

site_id	HC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE LMT D 363

Chain	Residue
B	GLU350
D	GLN98
D	GLY99
X	ILE21

site_id	HC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM F 85

Chain	Residue
F	HIS24
F	ALA27
F	ILE31
E	ARG8
E	PHE10
E	ILE13
E	ARG18
E	TYR19
E	HIS23
E	THR26
E	LEU30
F	PHE16
F	ARG19
F	TRP20

site_id	HC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SQD F 224

Chain	Residue
D	TRP21
D	ARG24
D	DGD362
F	PRO14
F	PHE16
F	THR17
F	VAL18
F	TRP20
X	ILE40

site_id	IC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA F 225

Chain	Residue
F	ARG45
V	GLU49

site_id	IC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE BCR X 107

Chain	Residue
B	CLA511
B	CLA512
B	CLA519
H	MET35
H	PHE38
H	PHE41
X	THR11
X	ILE12
X	LEU16
X	PHE20

site_id	IC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE DGD B 528

Chain	Residue
B	TYR193
B	PHE250
B	GLY254
B	TYR258
B	TYR273
B	SER277
B	PHE463
B	CLA512
D	GLY86
D	HIS87
D	PHE120
D	ILE159
D	LEU162
D	SER165
H	LEU46
H	TYR49
H	VAL60
H	SER61

site_id	IC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE LMG I 220

Chain	Residue
A	DGD375
I	LMT274

site_id	IC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BCR J 115

Chain	Residue
C	SQD475
C	LHG476
C	DGD492
J	VAL21
J	ILE22
J	PHE29
J	TYR30
J	TYR33
J	LMG492

site_id	IC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA K 56

Chain	Residue
K	ASP19
K	ASP23

site_id	IC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE BCR J 112

Chain	Residue
C	BCR489
J	ALA14
J	THR15
J	GLY18
J	MET19
K	LEU21
K	LEU31
K	PHE32
K	PHE37
K	VAL38
Z	SER16
Z	PHE17
y	ILE28
y	GLY29
y	GLY32

site_id	IC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE LMG M 217

Chain	Residue
L	SQD213
M	ILE23
M	GLU30
M	SER31

site_id	IC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE LMT T 226

Chain	Residue
M	MET1
T	MET1
T	PHE8

site_id	JC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA O 273

Chain	Residue
O	GLU140
O	HIS257

site_id	JC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE LMT I 274

Chain	Residue
A	ALA100
A	DGD375
I	MET1
I	LEU4
I	LMG220
O	LYS95

site_id	JC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SQD L 213

Chain	Residue
L	ARG14
L	LEU21
M	LMG217
T	PHE19

site_id	JC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE LMT O 274

Chain	Residue
A	DGD375

site_id	JC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM V 164

Chain	Residue
C	ALA393
V	ALA62
V	CYS63
V	CYS66
V	HIS67
V	THR74
V	ASN75
V	LEU78
V	LEU80
V	LEU85
V	TYR101
V	MET102
V	TYR108
V	HIS118

site_id	JC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE BCR Z 116

Chain	Residue
C	VAL116
C	SER121
C	LEU125
C	CLA487
C	CLA488
C	LMG494
K	TYR15
Z	VAL51
Z	VAL54
Z	GLY55
Z	ASN58

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	235
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	420
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	108
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	2
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	3
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	1
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	1
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	4
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	1
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	1
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Site: {"description":"Tyrosine radical intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11217865","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	1
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	129
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	226
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	46
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01496","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	332
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	237
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	115
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	1
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	1
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	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_FI29
Number of Residues	1
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_00643","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"16172937","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	4
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_FI31
Number of Residues	14
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	13
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	20
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_FI34
Number of Residues	2
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_FI35
Number of Residues	3
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)