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Ligands
Code Name Style Show Link
AZI Azide ion
CDL Cardiolipin
FES Fe2/s2 (inorganic) cluster
FNM (5s)-5-methyl-2-(methylsulfanyl)-5-phenyl-3-(phenylamino)-3,5-dihydro-4h-imidazol-4-one
HEC Heme C
HEM Protoporphyrin ix containing Fe
PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine
UNL Unknown ligand
UQ Coenzyme q10, (2z,6e,10z,14e,18e,22e,26z)-isomer
BOG Octyl beta-D-glucopyranoside
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 3L75   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : Cytochrome BC1 complex from chicken with fenamidone bound
Release Data : 2010-02-02
Compound :
mol_id molecule chains
1 MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN I A,N
ec: 1.10.2.2
mol_id molecule chains
2 MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN 2 B,O
ec: 1.10.2.2
mol_id molecule chains synonym
3 CYTOCHROME B C,P UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CYTOCHROME B SUBUNIT, CYTOCHROME B-C1 COMPLEX SUBUNIT 3, COMPLEX III SUBUNIT 3, COMPLEX III SUBUNIT III
ec: 1.10.2.2
mol_id molecule chains
4 MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN D,Q
ec: 1.10.2.2
mol_id molecule chains synonym
5 CYTOCHROME B-C1 COMPLEX SUBUNIT 5, RIESKE IRONSULFUR PROTEIN, MITOCHONDRIAL E,R UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, RIESKE IRON-SULFUR PROTEIN, RISP, COMPLEX III SUBUNIT 5
ec: 1.10.2.2
fragment: UNP RESIDUES 77-272
mol_id molecule chains
6 MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 14 KDA PROTEIN F,S
ec: 1.10.2.2
mol_id molecule chains
7 MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE UBIQUINONE-BINDING PROTEIN QP-C G,T
ec: 1.10.2.2
mol_id molecule chains
8 MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 11 KDA PROTEIN, COMPLEX III SUBUNIT VIII H,U
ec: 1.10.2.2
mol_id molecule chains synonym
9 CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL I,V UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, RIESKE IRON-SULFUR PROTEIN, RISP, COMPLEX III SUBUNIT 5
ec: 1.10.2.2
fragment: UNP RESIDUES 45-76
mol_id molecule chains
10 MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 7.2 KDA PROTEIN J,W
ec: 1.10.2.2
Source :
mol_id organism_scientific organism_common
1 GALLUS GALLUS  (taxid:9031) CHICKEN
mol_id organism_scientific organism_common
2 GALLUS GALLUS  (taxid:9031) CHICKEN
mol_id organism_scientific organism_common
3 GALLUS GALLUS  (taxid:9031) CHICKEN
mol_id organism_scientific organism_common
4 GALLUS GALLUS  (taxid:9031) CHICKEN
mol_id organism_scientific organism_common
5 GALLUS GALLUS  (taxid:9031) CHICKEN
mol_id organism_scientific organism_common
6 GALLUS GALLUS  (taxid:9031) CHICKEN
mol_id organism_scientific organism_common
7 GALLUS GALLUS  (taxid:9031) CHICKEN
mol_id organism_scientific organism_common
8 GALLUS GALLUS  (taxid:9031) CHICKEN
mol_id organism_scientific organism_common
9 GALLUS GALLUS  (taxid:9031) CHICKEN
mol_id organism_scientific organism_common
10 GALLUS GALLUS  (taxid:9031) CHICKEN
Authors : Huang, L., Berry, E.A.
Keywords : CYTOCHROME BC1, MEMBRANE PROTEIN, HEME PROTEIN, RIESKE IRON SULFUR PROTEIN, CYTOCHROME B, CYTOCHROME C1, COMPLEX III, MITOCHONDRIAL PROCESSING PROTEIN, UBIQUINONE, AZOXYSTROBIN OXIDOREDUCTASE, REDOX ENZYME RESPIRATORY CHAIN, ELECTRON TRANSPORT, HEME, INNER MEMBRANE, MEMBRANE, STROBILURINS BINDING, MITOCHONDRION, TRANSMEMBRANE, STIGMATELLIN, IRON, MITOCHONDRIAL INNER MEMBRANE, RESPIRATORY CHAIN, IRON-SULFUR, TRANSIT PEPTIDE, Metal-binding, Mitochondrion inner membrane, Transport, Disulfide bond, OXIDOREDUCTASE
Exp. method : X-RAY DIFFRACTION ( 2.79 Å )
Citation :

FAMOXADONE AND RELATED INHIBITORS BIND LIKE METHOXY ACRYLATE INHIBITORS IN THE Qo SITE OF THE BC1 COMPL AND FIX THE RIESKE IRON-SULFUR PROTEIN IN A POSITIO CLOSE TO BUT DISTINCT FROM THAT SEEN WITH STIGMATELLIN AND OTHER "DISTAL" Qo INHIBITORS.

Huang, L.,Berry, E.A.
To be Published 

Chain : A, N
UniProt : D0VX31 (D0VX31_CHICK)
Reaction : -
Chain : B, O
UniProt : D0VX29 (D0VX29_CHICK)
Reaction : -
Chain : C, P
UniProt : P18946 (CYB_CHICK)
Reaction : -
Chain : D, Q
UniProt : D0VX26 (D0VX26_CHICK)
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 ARBA:ARBA00029351
-
Chain : I, V
UniProt : Q5ZLR5 (UCRI_CHICK)
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 UniProtKB:P08067
-
Chain : F, S
UniProt : D0VX30 (D0VX30_CHICK)
Reaction : -
Chain : G, T
UniProt : D0VX32 (D0VX32_CHICK)
Reaction : -
Chain : H, U
UniProt : D0VX28 (D0VX28_CHICK)
Reaction : -
Chain : J, W
UniProt : D0VX27 (D0VX27_CHICK)
Reaction : -