Brand  (β version)

PDB ID: 1KB9

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Ligands
Code Name Style Show Link
CDL Cardiolipin PoSSuM
FES Fe2/s2 (inorganic) cluster PoSSuM
HEM Protoporphyrin ix containing Fe PoSSuM
PCF 1,2-diacyl-sn-glycero-3-phoshocholine PoSSuM
PEF Di-palmitoyl-3-sn-phosphatidylethanolamine PoSSuM
PIE 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoinositol PoSSuM
SMA Stigmatellin a PoSSuM
UMQ Undecyl-maltoside PoSSuM
UQ6 5-(3,7,11,15,19,23-hexamethyl-tetracosa-2,6,10,14,18,22-hexaenyl)-2,3-dimethoxy-6-methyl-benzene-1,4-diol PoSSuM
Non-standard Residues
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Structure summary

Code : 1KB9   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE/ELECTRON TRANSPORT
Title : YEAST CYTOCHROME BC1 COMPLEX
Release Data : 2002-09-18
Compound :
mol_id molecule chains
1 UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I A
ec: 1.10.2.2
fragment: RESIDUES 27-457
mol_id molecule chains
2 UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN 2 B
ec: 1.10.2.2
fragment: RESIDUES 17-368
mol_id molecule chains
3 CYTOCHROME B C
mol_id molecule chains
4 CYTOCHROME C1, HEME PROTEIN D
fragment: RESIDUES 62-307
mol_id molecule chains synonym
5 UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT E RIESKE IRON-SULFUR PROTEIN, RISP
ec: 1.10.2.2
fragment: RESIDUES 31-215
mol_id molecule chains synonym
6 UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 17 KD PROTEIN F MITOCHONDRIAL HINGE PROTEIN, COMPLEX III POLYPEPTIDE VI
ec: 1.10.2.2
fragment: RESIDUES 74-147
mol_id molecule chains synonym
7 UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 14 KD PROTEIN G COMPLEX III SUBUNIT VII
ec: 1.10.2.2
fragment: RESIDUES 3-127
mol_id molecule chains synonym
8 UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX UBIQUINONE-BINDING PROTEIN QP-C H UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 11 KDA PROTEIN, COMPLEX III SUBUNIT VIII
ec: 1.10.2.2
fragment: RESIDUES 2-94
mol_id molecule chains synonym
9 UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 7.3 KD PROTEIN I COMPLEX III POLYPEPTIDE IX
ec: 1.10.2.2
fragment: RESIDUES 4-58
mol_id molecule chains
10 HEAVY CHAIN (VH) OF FV-FRAGMENT J
mol_id molecule chains
11 LIGHT CHAIN (VL) OF FV-FRAGMENT K
Source :
mol_id organism_scientific organism_common
1 Saccharomyces cerevisiae  (taxid:4932) Baker's yeast
organelle: MITOCHONDRIA
mol_id organism_scientific organism_common
2 Saccharomyces cerevisiae  (taxid:4932) Baker's yeast
organelle: MITOCHONDRIA
mol_id organism_scientific organism_common
3 Saccharomyces cerevisiae  (taxid:4932) Baker's yeast
organelle: MITOCHONDRIA
mol_id organism_scientific organism_common
4 Saccharomyces cerevisiae  (taxid:4932) Baker's yeast
organelle: MITOCHONDRIA
mol_id organism_scientific organism_common
5 Saccharomyces cerevisiae  (taxid:4932) Baker's yeast
organelle: MITOCHONDRIA
mol_id organism_scientific organism_common
6 Saccharomyces cerevisiae  (taxid:4932) Baker's yeast
organelle: MITOCHONDRIA
mol_id organism_scientific organism_common
7 Saccharomyces cerevisiae  (taxid:4932) Baker's yeast
organelle: MITOCHONDRIA
mol_id organism_scientific organism_common
8 Saccharomyces cerevisiae  (taxid:4932) Baker's yeast
organelle: MITOCHONDRIA
mol_id organism_scientific organism_common
9 Saccharomyces cerevisiae  (taxid:4932) Baker's yeast
organelle: MITOCHONDRIA
mol_id organism_scientific organism_common expression_system
10 Mus musculus  (taxid:10090) House mouse Escherichia coli  (taxid:562)
mol_id organism_scientific organism_common expression_system
11 Mus musculus  (taxid:10090) House mouse Escherichia coli  (taxid:562)
expression_system_strain: JM83
expression_system_vector_type: plasmid
expression_system_plasmid: pASK68
Authors : Lange, C., Nett, J.H., Trumpower, B.L., Hunte, C.
Keywords : oxidoreductase, ubiquinone, stigmatellin, cardiolipin, phosphatidylinositol, phosphatidylcholin, phosphatidylethanolamin, undecyl-maltopyranoside, OXIDOREDUCTASE-ELECTRON TRANSPORT COMPLEX
Exp. method : X-RAY DIFFRACTION ( 2.30 Å )
Citation :

SPECIFIC ROLES OF PROTEIN-PHOSPHOLIPID INTERACTIONS IN THE YEAST CYTOCHROME BC1 COMPLEX STRUCTURE

Lange, C.,Nett, J.H.,Trumpower, B.L.  et al.
(2001)  EMBO J.  20 : 6591 - 6600

PubMed: 11726495
DOI: 10.1093/emboj/20.23.6591

Structure Of The Yeast Cytochrome Bc1 Complex Co-Crystallized With An Antibody Fv-Fragment

Hunte, C.,Koepke, J.,Lange, C.  et al.
(2000)  Structure  8 : 669 - 684

DOI: 10.1016/S0969-2126(00)00152-0

Reaction

Chain : A
UniProt : P07256 (QCR1_YEAST)
Reaction : -
Chain : B
UniProt : P07257 (QCR2_YEAST)
Reaction : -
Chain : C
UniProt : P00163 (CYB_YEAST)
Reaction: EC: Evidence:
Physiological Direction:
a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out) 7.1.1.8 PubMed:2551731, PubMed:8031140
-
Cofactor: Evidence: Note:
heme b ECO:0000269 | PubMed:10873857
ECO:0000269 | PubMed:11880631
ECO:0000269 | PubMed:18390544
ECO:0000269 | PubMed:30598554
Binds 2 heme b groups non-covalently per subunit.
Chain : D
UniProt : P07143 (CY1_YEAST)
Reaction: EC: Evidence:
Physiological Direction:
a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out) 7.1.1.8 PubMed:11279090
-
Cofactor: Evidence: Note:
heme c ECO:0000269 | PubMed:18390544
ECO:0000269 | PubMed:30598554
Binds 1 heme c group covalently per subunit.
Chain : E
UniProt : P08067 (UCRI_YEAST)
Reaction: EC: Evidence:
Physiological Direction:
a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out) 7.1.1.8 PubMed:1657998, PubMed:2538628
-
Cofactor: Evidence: Note:
[2Fe-2S] cluster ECO:0000269 | PubMed:10873857
ECO:0000269 | PubMed:11880631
ECO:0000269 | PubMed:18390544
ECO:0000269 | PubMed:30598554
Binds 1 [2Fe-2S] cluster per subunit.
Chain : F
UniProt : P00127 (QCR6_YEAST)
Reaction : -
Chain : G
UniProt : P00128 (QCR7_YEAST)
Reaction : -
Chain : H
UniProt : P08525 (QCR8_YEAST)
Reaction : -
Chain : I
UniProt : P22289 (QCR9_YEAST)
Reaction : -