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4H0L

Cytochrome b6f Complex Crystal Structure from Mastigocladus laminosus with n-Side Inhibitor NQNO

Functional Information from GO Data
ChainGOidnamespacecontents
A0009055molecular_functionelectron transfer activity
A0009579cellular_componentthylakoid
A0015979biological_processphotosynthesis
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0022904biological_processrespiratory electron transport chain
A0031676cellular_componentplasma membrane-derived thylakoid membrane
A0042651cellular_componentthylakoid membrane
A0046872molecular_functionmetal ion binding
B0008121molecular_functionubiquinol-cytochrome-c reductase activity
B0009055molecular_functionelectron transfer activity
B0009579cellular_componentthylakoid
B0009767biological_processphotosynthetic electron transport chain
B0015979biological_processphotosynthesis
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0031676cellular_componentplasma membrane-derived thylakoid membrane
B0042651cellular_componentthylakoid membrane
B1902600biological_processproton transmembrane transport
C0005506molecular_functioniron ion binding
C0009055molecular_functionelectron transfer activity
C0009579cellular_componentthylakoid
C0015979biological_processphotosynthesis
C0016020cellular_componentmembrane
C0020037molecular_functionheme binding
C0031676cellular_componentplasma membrane-derived thylakoid membrane
C0042651cellular_componentthylakoid membrane
C0046872molecular_functionmetal ion binding
D0004497molecular_functionmonooxygenase activity
D0009496molecular_functionplastoquinol--plastocyanin reductase activity
D0009579cellular_componentthylakoid
D0015979biological_processphotosynthesis
D0016020cellular_componentmembrane
D0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
D0031676cellular_componentplasma membrane-derived thylakoid membrane
D0046872molecular_functionmetal ion binding
D0051536molecular_functioniron-sulfur cluster binding
D0051537molecular_function2 iron, 2 sulfur cluster binding
D0055085biological_processtransmembrane transport
E0009055molecular_functionelectron transfer activity
E0009512cellular_componentcytochrome b6f complex
E0009579cellular_componentthylakoid
E0015979biological_processphotosynthesis
E0016020cellular_componentmembrane
E0031676cellular_componentplasma membrane-derived thylakoid membrane
E0042651cellular_componentthylakoid membrane
F0009055molecular_functionelectron transfer activity
F0009512cellular_componentcytochrome b6f complex
F0009579cellular_componentthylakoid
F0015979biological_processphotosynthesis
F0016020cellular_componentmembrane
F0031676cellular_componentplasma membrane-derived thylakoid membrane
F0042651cellular_componentthylakoid membrane
G0009512cellular_componentcytochrome b6f complex
G0009579cellular_componentthylakoid
G0015979biological_processphotosynthesis
G0016020cellular_componentmembrane
G0017004biological_processcytochrome complex assembly
G0031676cellular_componentplasma membrane-derived thylakoid membrane
G0042651cellular_componentthylakoid membrane
H0009055molecular_functionelectron transfer activity
H0009512cellular_componentcytochrome b6f complex
H0009579cellular_componentthylakoid
H0015979biological_processphotosynthesis
H0016020cellular_componentmembrane
H0017004biological_processcytochrome complex assembly
H0031676cellular_componentplasma membrane-derived thylakoid membrane
H0042651cellular_componentthylakoid membrane
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 301
ChainResidue
AGLU75
AHOH401
CLYS140
CHIS143

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM A 302
ChainResidue
AHIS86
AARG87
AALA90
AMET93
APHE131
AGLY135
ALEU138
APRO139
AHIS187
ATHR188
APHE189
AGLN47
AGLY51
APHE52
AMET54
AARG83

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM A 303
ChainResidue
ATYR34
AGLY37
AGLY38
AMET93
AHIS100
AVAL101
AARG103
AVAL104
AGLY109
AARG114
ATHR117
ATRP118
AGLY121
AVAL122
AALA125
AHIS202
APHE203
AILE206
AILE211
ASER212
AHEM304
AHOH402

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM A 304
ChainResidue
AVAL30
ATYR34
ACYS35
AGLY38
ALEU41
APHE203
AILE206
AARG207
AGLY210
AILE211
AHEM303
AQNO308
AHOH402
BASN25
BVAL39
BPHE40
HARG26

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE OPC A 305
ChainResidue
AMET92
BCYS50
CGLN38
ETYR8
FGLU3
FTYR7
FVAL18
GLEU5
GLEU9
GBCR101
HTRP8
HPHE15

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UMQ A 306
ChainResidue
ALEU12
AASP20
ALYS24
ALYS208

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE UMQ A 307
ChainResidue
ATYR5
AASP6
AILE14
AGLN15
AUMQ309

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE QNO A 308
ChainResidue
ALYS24
AARG207
AHEM304
BLEU36
BPHE40

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UMQ A 309
ChainResidue
AUMQ307
BTRP32
CGLU286
DSQD201

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD B 201
ChainResidue
BASP58
CLYS146
FGLU4

site_idBC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE CLA B 202
ChainResidue
BLEU108
BILE132
BPHE133
BGLY136
BTHR140
BOPC203
BHOH301
BHOH303
ATYR105
BTYR80
BVAL84
BILE87
BMET101
BVAL104
BPRO105

site_idBC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE OPC B 203
ChainResidue
ATYR105
BLEU100
BSER103
BVAL111
BILE114
BGLU115
BASN118
BARG126
BPRO127
BVAL128
BALA129
BCLA202

site_idBC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE UMQ C 301
ChainResidue
AASN74
AGLU75
ATRP80
CASP251
CASN253
CTRP257
DGLY33
DALA34
DPRO37

site_idBC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM C 302
ChainResidue
CTYR1
CPRO2
CTRP4
CALA5
CCYS22
CCYS25
CHIS26
CGLN60
CLEU70
CASN71
CVAL72
CGLY73
CALA74
CASN154
CGLY156
CARG157
CGLY158
CILE160
CTYR161

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FES D 200
ChainResidue
DCYS108
DHIS110
DLEU111
DCYS126
DHIS129
DGLY130
DSER131

site_idBC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SQD D 201
ChainResidue
AUMQ309
BTRP32
BPRO33
BLEU37
BTYR38
CLYS275
CVAL279
DARG16
DASN20
DPHE24
DGLY25
DTHR28

site_idBC8
Number of Residues14
DetailsBINDING SITE FOR RESIDUE BCR G 101
ChainResidue
AILE32
APHE33
AILE39
AMET96
ALEU99
AOPC305
FILE16
FPHE17
FTRP20
GALA16
GGLY19
GGLY20
GTYR23
HPHE15

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsTRANSMEM: Helical => ECO:0000255|HAMAP-Rule:MF_00395, ECO:0000305|PubMed:14526088
ChainResidueDetails
HILE3-VAL23
BASN116-THR130
AARG207-LEU215

site_idSWS_FT_FI2
Number of Residues22
DetailsTRANSMEM: Helical => ECO:0000305|PubMed:14526088
ChainResidueDetails
DLEU21-ILE43
BLEU95-GLU115
BTHR131-LEU151
AALA186-ILE206

site_idSWS_FT_FI3
Number of Residues135
DetailsTOPO_DOM: Lumenal, thylakoid => ECO:0000305|PubMed:14526088
ChainResidueDetails
DPRO44-VAL179
CHIS26

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:14526088
ChainResidueDetails
DCYS108
DHIS110
DCYS126
DHIS129

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:14526088, ECO:0000269|PubMed:16371475, ECO:0007744|PDB:1VF5, ECO:0007744|PDB:2D2C
ChainResidueDetails
AARG83

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:14526088, ECO:0000269|PubMed:16371475, ECO:0007744|PDB:1VF5, ECO:0007744|PDB:2D2C
ChainResidueDetails
AHIS86
AHIS100
AHIS187
AHIS202

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:14526088, ECO:0007744|PDB:1VF5
ChainResidueDetails
AARG103
ALYS208

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PDB entries from 2025-06-11

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