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Ligands
Code Name Style Show Link
HEM Protoporphyrin ix containing Fe
FMX Famoxadone
SR Strontium ion
LOP (1r)-2-{[(R)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(dodecanoyloxy)methyl]ethyl (9z)-octadec-9-enoate
HEC Heme C
FES Fe2/s2 (inorganic) cluster
ASC Ascorbic acid
BOG Octyl beta-D-glucopyranoside
Non-standard Residues
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Glycosylation
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Code : 5KKZ   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : Rhodobacter sphaeroides bc1 with famoxadone
Release Data : 2016-10-12
Compound :
mol_id molecule chains
1 Cytochrome b A,E,K,O
mol_id molecule chains
2 Cytochrome c1 B,F,L,P
mol_id molecule chains synonym
3 Ubiquinol-cytochrome c reductase iron-sulfur subunit C,G,M,Q Rieske iron-sulfur protein,RISP
ec: 1.10.2.2
Source :
mol_id organism_scientific expression_system
1 Rhodobacter sphaeroides  (taxid:1063) Rhodobacter sp.  (taxid:1062)
gene: petB, fbcB
mol_id organism_scientific expression_system
2 Rhodobacter sphaeroides  (taxid:1063) Rhodobacter sp.  (taxid:1062)
gene: petC, fbcC
mol_id organism_scientific expression_system
3 Rhodobacter sphaeroides  (taxid:1063) Rhodobacter sp.  (taxid:1062)
gene: petA, fbcF
Authors : Xia, D., Esser, L., Zhou, F., Tang, W.K., Yu, C.A.
Keywords : Mitochondrial respiratory chain complex, cytochrome bc1, inhibitors, electron transfer, OXIDOREDUCTASE
Exp. method : X-RAY DIFFRACTION ( 2.970 Å )
Citation :

Hydrogen Bonding to the Substrate Is Not Required for Rieske Iron-Sulfur Protein Docking to the Quinol Oxidation Site of Complex III.

Esser, L.,Zhou, F.,Zhou, Y.  et al.
(2016)  J.Biol.Chem.  291 : 25019 - 25031

PubMed: 27758861
DOI: 10.1074/jbc.M116.744391

Chain : A, E, K, O
UniProt : Q02761 (CYB_CERSP)
Reaction : -
Chain : B, F, L, P
UniProt : Q02760 (CY1_CERSP)
Reaction : -
Chain : C, G, M, Q
UniProt : Q02762 (UCRI_CERSP)
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 -
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