Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4I7Z

Crystal structure of cytochrome b6f in DOPG, with disordered Rieske Iron-Sulfur Protein soluble domain

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	0008121	molecular_function	quinol-cytochrome-c reductase activity
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
B	1902600	biological_process	proton transmembrane transport
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	0031676	cellular_component	plasma membrane-derived thylakoid membrane
C	0042651	cellular_component	thylakoid membrane
C	0046872	molecular_function	metal ion binding
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	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	17
Details	BINDING SITE FOR RESIDUE HEM A 301

Chain	Residue
A	GLN47
A	ALA90
A	THR128
A	PHE131
A	GLY135
A	LEU138
A	PRO139
A	HIS187
A	PHE189
A	PHE48
A	GLY51
A	PHE52
A	MET54
A	TYR58
A	ARG83
A	HIS86
A	ARG87

site_id	AC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE HEM A 302

Chain	Residue
A	TYR34
A	GLY37
A	GLY38
A	THR40
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	HEM303
A	HOH401
A	HOH402
A	HOH403

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM A 303

Chain	Residue
A	TYR34
A	CYS35
A	GLY38
A	THR42
A	ILE206
A	ARG207
A	GLY210
A	ILE211
A	HEM302
A	HOH401
B	ASN25
B	ASP35
B	PHE40
B	ILE44
H	ARG26

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MYS A 304

Chain	Residue
A	LEU169
A	ALA186

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE 8K6 A 305

Chain	Residue
A	PHE52
A	MET199

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE UMQ A 306

Chain	Residue
A	LEU12
A	GLU13
A	ALA16
A	LEU17
A	ILE119
A	LEU204
A	LYS208

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE UMQ A 307

Chain	Residue
A	TYR5
A	ASP6
A	ILE14
A	GLN15
A	ALA18
A	UMQ308

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE UMQ A 308

Chain	Residue
A	ALA18
A	UMQ307
C	GLU286
D	1E2201

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CD A 309

Chain	Residue
A	GLU75
C	HIS143
C	HOH401

site_id	BC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CLA B 201

Chain	Residue
A	TYR105
A	ALA125
A	VAL129
B	TYR80
B	PRO83
B	VAL84
B	ILE87
B	MET101
B	ILE132
B	PHE133
B	GLY136
B	VAL139
B	THR140
B	OZ2203
B	HOH301
B	HOH302

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD B 202

Chain	Residue
G	GLU3
B	ASP58
C	LYS146
F	GLU4

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE OZ2 B 203

Chain	Residue
A	TYR105
B	SER103
B	GLU115
B	ASN118
B	ARG126
B	VAL128
B	ALA129
B	CLA201

site_id	BC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEM C 301

Chain	Residue
C	TYR1
C	TRP4
C	ALA5
C	CYS22
C	CYS25
C	HIS26
C	GLN60
C	LEU70
C	ASN71
C	VAL72
C	GLY73
C	ALA74
C	ASN154
C	GLY156
C	ARG157
C	GLY158
C	ILE160
C	TYR161

site_id	BC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CD C 302

Chain	Residue
C	HIS150

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE OZ2 C 303

Chain	Residue
A	PHE78
A	TRP80
C	ASN253
C	TRP257

site_id	BC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 1E2 D 201

Chain	Residue
A	UMQ308
B	TRP32
B	PRO33
B	TYR38
C	LYS275
C	VAL279
D	ARG16
D	ASN20
D	PHE24

site_id	BC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE BCR G 101

Chain	Residue
A	ILE32
A	PHE33
A	ILE39
A	MET96
A	LEU99
F	ILE16
F	PHE17
G	ALA16
G	GLY19
G	GLY20
G	TYR23
G	OZ2102
H	ILE19

site_id	BC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE OZ2 G 102

Chain	Residue
A	MET92
C	PRO37
C	GLN38
E	TYR8
F	TYR7
G	LEU5
G	LEU9
G	BCR101
H	TRP8
H	LEU12
H	PHE15

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"},{"source":"PubMed","id":"14526088","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	129
Details	Topological domain: {"description":"Lumenal, thylakoid","evidences":[{"source":"PubMed","id":"14526088","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	26
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"14526088","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"14526088","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16371475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1VF5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2D2C","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14526088","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16371475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1VF5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2D2C","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"14526088","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16371475","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1VF5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2D2C","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14526088","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1VF5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	60
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_01344","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14526088","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	42
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"14526088","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"14526088","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"14526088","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	20
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00433","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14526088","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	20
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00396","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14526088","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	20
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00432","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14526088","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	20
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00395","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14526088","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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