Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4PV1

Cytochrome B6F structure from M. laminosus with the quinone analog inhibitor stigmatellin

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	4
Details	BINDING SITE FOR RESIDUE MYS A 301

Chain	Residue
A	SER130
A	THR134
A	LEU169
A	ALA186

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD A 302

Chain	Residue
A	GLU75
C	HIS143
C	HOH1101
C	HOH1102

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEC A 303

Chain	Residue
A	GLN47
A	PHE48
A	GLY51
A	PHE52
A	MET54
A	ARG83
A	HIS86
A	ALA90
A	MET93
A	PHE131
A	GLY135
A	LEU138
A	PRO139
A	HIS187
A	THR188
A	PHE189
A	PHE44

site_id	AC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEC A 304

Chain	Residue
A	TYR34
A	GLY37
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	HEC305
A	HOH401
A	HOH402

site_id	AC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEC A 305

Chain	Residue
A	ASN31
A	TYR34
A	CYS35
A	GLY38
A	THR42
A	ILE206
A	ARG207
A	GLY210
A	ILE211
A	HEC304
A	SMA308
A	HOH401
B	ASN25
B	PHE40
H	ARG26

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE UMQ A 306

Chain	Residue
A	LEU12
A	LEU17
A	LYS208
A	UMQ307

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE UMQ A 307

Chain	Residue
A	ASP6
A	ILE14
A	GLN15
A	ALA18
A	UMQ306
B	UMQ203
D	OPC203

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SMA A 308

Chain	Residue
A	LYS24
A	ARG207
A	HEC305
B	LEU36
B	PHE40
B	UMQ203

site_id	AC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 7PH A 309

Chain	Residue
A	PHE78
B	PHE48
B	8K6201
C	ARG254
C	TRP257
C	PHE261
D	GLY33
D	ALA34
D	TYR36
D	PRO37

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE 8K6 B 201

Chain	Residue
A	7PH309
B	PHE48
D	ALA34

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

Chain	Residue
B	ASP58
C	LYS146
G	GLU3

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE UMQ B 203

Chain	Residue
D	SQD202
A	THR22
A	UMQ307
A	SMA308
B	TRP32

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

Chain	Residue
A	PHE102
A	TYR105
A	ALA125
B	TYR80
B	VAL84
B	ILE87
B	VAL104
B	PHE133
B	GLY136
B	VAL139
B	THR140
B	OPC205
B	HOH301
B	HOH305

site_id	BC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE OPC B 205

Chain	Residue
A	TYR105
B	SER103
B	VAL111
B	GLU115
B	ASN118
B	ARG126
B	PRO127
B	VAL128
B	ALA129
B	ILE132
B	CLA204

site_id	BC6
Number of Residues	19
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	ASN154
C	GLY156
C	ARG157
C	GLY158
C	ILE160
C	TYR161

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES D 201

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

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SQD D 202

Chain	Residue
B	TRP32
B	PRO33
B	UMQ203
C	LYS275
D	ARG16
D	ASN20

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE OPC D 203

Chain	Residue
A	UMQ307
D	LEU38

site_id	CC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE OPC E 101

Chain	Residue
A	MET92
B	CYS50
C	GLN38
E	GLY4
E	ALA5
E	TYR8
F	TYR7
F	ALA8
F	LEU11
F	GLY14
G	LEU5
G	LEU9
G	BCR101
H	TRP8
H	LEU12
H	PHE15

site_id	CC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE BCR G 101

Chain	Residue
A	PHE33
A	ILE39
E	OPC101
F	ILE16
F	PHE17
F	TRP20
G	ALA16
G	GLY19
G	GLY20
G	TYR23

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	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14526088","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
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_FI14
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_FI15
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_FI16
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)