Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4OGQ

Internal Lipid Architecture of the Hetero-Oligomeric Cytochrome b6f Complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0009055	molecular_function	electron transfer activity
A	0015979	biological_process	photosynthesis
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0022904	biological_process	respiratory electron transport chain
A	0031676	cellular_component	plasma membrane-derived thylakoid membrane
A	0042651	cellular_component	thylakoid membrane
A	0046872	molecular_function	metal ion binding
B	0009055	molecular_function	electron transfer activity
B	0009767	biological_process	photosynthetic electron transport chain
B	0015979	biological_process	photosynthesis
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0031676	cellular_component	plasma membrane-derived thylakoid membrane
B	0042651	cellular_component	thylakoid membrane
C	0005506	molecular_function	iron ion binding
C	0009055	molecular_function	electron transfer activity
C	0015979	biological_process	photosynthesis
C	0020037	molecular_function	heme binding
C	0042651	cellular_component	thylakoid membrane
D	0004497	molecular_function	monooxygenase activity
D	0009496	molecular_function	plastoquinol--plastocyanin reductase activity
D	0015979	biological_process	photosynthesis
D	0016020	cellular_component	membrane
D	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
D	0031676	cellular_component	plasma membrane-derived thylakoid membrane
D	0042651	cellular_component	thylakoid membrane
D	0046872	molecular_function	metal ion binding
D	0051536	molecular_function	iron-sulfur cluster binding
D	0051537	molecular_function	2 iron, 2 sulfur cluster binding
D	0055085	biological_process	transmembrane transport
E	0009055	molecular_function	electron transfer activity
E	0009512	cellular_component	cytochrome b6f complex
E	0015979	biological_process	photosynthesis
E	0031676	cellular_component	plasma membrane-derived thylakoid membrane
E	0042651	cellular_component	thylakoid membrane
F	0009055	molecular_function	electron transfer activity
F	0009512	cellular_component	cytochrome b6f complex
F	0015979	biological_process	photosynthesis
F	0031676	cellular_component	plasma membrane-derived thylakoid membrane
F	0042651	cellular_component	thylakoid membrane
G	0009512	cellular_component	cytochrome b6f complex
G	0015979	biological_process	photosynthesis
G	0017004	biological_process	cytochrome complex assembly
G	0031676	cellular_component	plasma membrane-derived thylakoid membrane
G	0042651	cellular_component	thylakoid membrane
H	0009055	molecular_function	electron transfer activity
H	0009512	cellular_component	cytochrome b6f complex
H	0015979	biological_process	photosynthesis
H	0017004	biological_process	cytochrome complex assembly
H	0031676	cellular_component	plasma membrane-derived thylakoid membrane
H	0042651	cellular_component	thylakoid membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEC A 301

Chain	Residue
A	GLN47
A	GLY135
A	LEU138
A	PRO139
A	HIS187
A	PHE189
B	GLU78
A	PHE48
A	GLY51
A	MET54
A	ARG83
A	HIS86
A	ARG87
A	ALA90
A	PHE131

site_id	AC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEC A 302

Chain	Residue
A	TYR34
A	GLY37
A	GLY38
A	MET93
A	HIS100
A	VAL101
A	ARG103
A	VAL104
A	GLY109
A	ARG114
A	THR117
A	TRP118
A	GLY121
A	MET199
A	HIS202
A	PHE203
A	ILE206
A	ILE211
A	SER212
A	HEC303
A	HOH401
A	HOH406

site_id	AC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEC A 303

Chain	Residue
A	TYR34
A	CYS35
A	GLY38
A	LEU41
A	ARG207
A	GLY210
A	ILE211
A	HEC302
A	HOH401
A	HOH410
A	HOH416
A	HOH417
B	ASN25
B	PHE40
B	UMQ203
H	ARG26

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE UMQ A 304

Chain	Residue
A	TYR5
B	UMQ201
D	SQD204

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE 7PH A 305

Chain	Residue
A	VAL4
A	TRP7
B	PHE113

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE 8K6 A 306

Chain	Residue
A	VAL197
A	LEU200
A	PHE201
A	8K6307
A	8K6308
B	CLA204

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE 8K6 A 307

Chain	Residue
A	MET205
A	LYS208
A	8K6306

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 8K6 A 308

Chain	Residue
A	SER130
A	THR134
A	LEU169
A	ALA186
A	8K6306

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 2WM A 309

Chain	Residue
A	LEU45
A	PHE52
A	LEU194
A	PHE203
D	VAL38

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE UMQ B 201

Chain	Residue
A	ALA18
A	GLU19
A	THR22
A	UMQ304
B	TRP32
C	ASN288
D	SQD204

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE 8K6 B 202

Chain	Residue
B	LEU36
B	PHE40
B	PRO41

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE UMQ B 203

Chain	Residue
A	LYS24
A	ARG207
A	HEC303
B	ALA31
B	LEU36
B	PHE40
B	PRO41
B	HOH301

site_id	BC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CLA B 204

Chain	Residue
A	8K6306
B	TYR80
B	VAL84
B	LEU108
B	PHE133
B	GLY136
B	THR140
B	OPC205
B	HOH308
B	HOH316
F	2WA101
A	PHE102
A	TYR105
A	VAL129

site_id	BC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE OPC B 205

Chain	Residue
A	TYR105
B	ALA100
B	SER103
B	VAL111
B	ILE114
B	GLU115
B	ASN118
B	ARG126
B	PRO127
B	VAL128
B	ALA129
B	CLA204
B	HOH306

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 7PH B 206

Chain	Residue
B	PHE124
B	THR130
B	THR131
B	LEU134
G	PHE22

site_id	BC7
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEC C 301

Chain	Residue
C	TYR1
C	PRO2
C	TRP4
C	ALA5
C	CYS22
C	CYS25
C	HIS26
C	GLN60
C	LEU70
C	ASN71
C	VAL72
C	GLY73
C	ALA74
C	VAL75
C	ASN154
C	GLY156
C	ARG157
C	GLY158
C	VAL160
C	TYR161
C	HOH435

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CD C 302

Chain	Residue
A	GLU75
C	LYS140
C	HIS143

site_id	BC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 7PH C 303

Chain	Residue
C	ALA252
C	ASN253
C	GLY256
C	TRP257
C	ALA260
E	PHE10
H	ILE3

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE UMQ D 201

Chain	Residue
D	GLY14
D	PHE18
D	LEU22
E	LEU25

site_id	CC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MYS D 202

Chain	Residue
A	LEU168
D	PHE42

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 7PH D 203

Chain	Residue
C	ASP251
C	TRP257
C	PHE261
D	GLY33
D	TYR36

site_id	CC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE SQD D 204

Chain	Residue
A	UMQ304
B	TRP32
B	TYR38
B	UMQ201
B	HOH307
C	LYS275
D	ARG16
D	ASN20
D	PHE24
D	GLY25
D	THR28
D	GLY29

site_id	CC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES D 205

Chain	Residue
D	CYS108
D	HIS110
D	LEU111
D	CYS126
D	HIS129
D	SER131

site_id	CC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE 2WD D 206

Chain	Residue
D	TYR36
D	VAL39
D	ILE43

site_id	CC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 3WM E 101

Chain	Residue
A	CYS43
A	MET92
A	MET96
C	GLN38
C	SER39
E	ALA3
E	ILE4
E	TYR7
E	ILE8
F	GLU4
F	1O2103
H	THR5
H	TRP8
H	LEU12
H	PHE15

site_id	CC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 2WA F 101

Chain	Residue
B	CLA204
F	MET1
F	SER2
F	LEU5
F	ALA9
F	PHE13
G	VAL2
G	ILE14

site_id	CC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE OCT F 102

Chain	Residue
F	ASN7
F	LEU10

site_id	DC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 1O2 F 103

Chain	Residue
E	ILE8
E	ALA12
E	GLY16
E	PHE23
E	3WM101
F	LYS28
F	ILE29
F	GLY31

site_id	DC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 7PH F 104

Chain	Residue
F	PHE17
F	TRP20
F	ALA24
G	TYR23
G	BCR102

site_id	DC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE UMQ G 101

Chain	Residue
G	TYR26
G	TYR29
G	LYS30

site_id	DC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE BCR G 102

Chain	Residue
A	ILE32
A	PHE33
A	ILE39
A	MET96
F	ILE16
F	PHE17
F	TRP20
F	7PH104
G	VAL16
G	ALA19
G	GLY20
G	TYR23
H	PHE15
H	SER18
H	ILE19

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	80
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00633","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"description":"covalent","evidences":[{"source":"HAMAP-Rule","id":"MF_00633","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_00633","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	60
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_01344","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	19
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00610","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_00610","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"description":"covalent","evidences":[{"source":"HAMAP-Rule","id":"MF_00610","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	22
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_01335","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01335","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	20
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00433","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	20
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00396","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	20
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00432","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	20
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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