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2YIU

X-ray structure of the dimeric cytochrome BC1 complex from the soil bacterium paracoccus denitrificans at 2.7 angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0008121molecular_functionquinol-cytochrome-c reductase activity
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0022904biological_processrespiratory electron transport chain
A0045275cellular_componentrespiratory chain complex III
A0046872molecular_functionmetal ion binding
A1902600biological_processproton transmembrane transport
B0009055molecular_functionelectron transfer activity
B0020037molecular_functionheme binding
C0005886cellular_componentplasma membrane
C0008121molecular_functionquinol-cytochrome-c reductase activity
C0016020cellular_componentmembrane
C0046872molecular_functionmetal ion binding
C0051536molecular_functioniron-sulfur cluster binding
C0051537molecular_function2 iron, 2 sulfur cluster binding
C1902600biological_processproton transmembrane transport
D0005886cellular_componentplasma membrane
D0008121molecular_functionquinol-cytochrome-c reductase activity
D0009055molecular_functionelectron transfer activity
D0016020cellular_componentmembrane
D0016491molecular_functionoxidoreductase activity
D0022904biological_processrespiratory electron transport chain
D0045275cellular_componentrespiratory chain complex III
D0046872molecular_functionmetal ion binding
D1902600biological_processproton transmembrane transport
E0009055molecular_functionelectron transfer activity
E0020037molecular_functionheme binding
F0005886cellular_componentplasma membrane
F0008121molecular_functionquinol-cytochrome-c reductase activity
F0016020cellular_componentmembrane
F0046872molecular_functionmetal ion binding
F0051536molecular_functioniron-sulfur cluster binding
F0051537molecular_function2 iron, 2 sulfur cluster binding
F1902600biological_processproton transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM A 500
ChainResidue
AGLN58
ALEU149
APRO150
AHIS198
APRO202
AGLY62
AILE63
AVAL66
AARG94
AHIS97
APHE104
ATHR142
AGLY146

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 501
ChainResidue
ATRP45
AGLY48
ALEU51
AALA52
AHIS111
AARG114
ASER120
AARG125
ATRP129
AGLY132
AMET133
AILE135
AHIS212
APHE216
AGLY220
AASN221
AASN222
AHOH2002

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE SMA A 502
ChainResidue
ALEU137
AMET154
AGLY158
AVAL161
APHE194
AILE292
AGLU295
APHE298
ATYR302
AMET336
APHE337
FCYS154
FHIS155

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HEC B 500
ChainResidue
BVAL81
BCYS82
BCYS85
BHIS86
BPRO145
BARG154
BTYR177
BLEU182
BPHE203
BGLN209
BMET210

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES C 500
ChainResidue
CCYS132
CHIS134
CLEU135
CCYS152
CHIS155
CSER157

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM D 500
ChainResidue
DGLN58
DGLY62
DILE63
DVAL66
DARG94
DHIS97
DALA98
DPHE104
DGLY146
DLEU149
DPRO150
DHIS198
DPRO202

site_idAC7
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM D 501
ChainResidue
DTRP45
DGLY48
DLEU51
DALA52
DHIS111
DARG114
DSER120
DARG125
DGLY132
DMET133
DILE135
DVAL209
DHIS212
DPHE216
DGLY220
DASN221
DASN222

site_idAC8
Number of Residues13
DetailsBINDING SITE FOR RESIDUE SMA D 502
ChainResidue
DPHE298
DTYR302
DMET336
DPHE337
DILE340
CCYS154
CHIS155
DLEU137
DMET140
DVAL161
DILE292
DPRO294
DGLU295

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HEC E 500
ChainResidue
EVAL81
ECYS82
ECYS85
EHIS86
EARG154
ETYR177
EPHE203
EGLN209
EMET210
EPRO213

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES F 500
ChainResidue
FCYS132
FHIS134
FLEU135
FCYS152
FHIS155
FSER157

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues440
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues28
DetailsTransmembrane: {"description":"Helical; Note=Anchors to the membrane","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues42
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"description":"covalent"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues186
DetailsDomain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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