Brand  (β version)

PDB ID: 3H1J

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Ligands
Code Name Style Show Link
CDL Cardiolipin PoSSuM
FES Fe2/s2 (inorganic) cluster PoSSuM
GOL Glycerol PoSSuM
HEC Heme C PoSSuM
HEM Protoporphyrin ix containing Fe PoSSuM
PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine PoSSuM
PLC Diundecyl phosphatidyl choline PoSSuM
SMA Stigmatellin a PoSSuM
UNL Unknown ligand PoSSuM
UQ Coenzyme q10, (2z,6e,10z,14e,18e,22e,26z)-isomer PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
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Structure summary

Code : 3H1J   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : Stigmatellin-bound cytochrome bc1 complex from chicken
Release Data : 2009-04-28
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 Rieske, 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: sequence database 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: sequence database residues 1-76
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 : Zhang, Z., Huang, L., Shulmeister, V.M., Chi, Y.-I., Kim, K.K., Hung, L.-W., Crofts, A.R., Berry, E.A., Kim, S.-H.
Keywords : CYTOCHROME BC1, MEMBRANE PROTEIN, HEME PROTEIN, RIESKE IRON SULFUR PROTEIN, CYTOCHROME B, CYTOCHROME C1, COMPLEX III, MITOCHONDRIAL PROCESSING PROTEIN, UBIQUINONE, OXIDOREDUCTASE, REDOX ENZYM RESPIRATORY CHAIN, ELECTRON TRANSPORT, HEME, INNER MEMBRANE IRON, MEMBRANE, METAL-BINDING, MITOCHONDRION, TRANSMEMBRANE, stigmatellin, Iron, Mitochondrion inner membrane, Respiratory chain, Transport, Disulfide bond, Iron-sulfur, Transit peptide
Exp. method : X-RAY DIFFRACTION ( 3.00 Å )
Citation :

Electron Transfer by Domain Movement in Cytochrome Bc1

Zhang, Z.,Huang, L.-S.,Shulmeister, V.M.  et al.
(1998)  Nature  392 : 677 - 684

PubMed: 9565029

Structure of the avian mitochondrial cytochrome bc1 complex

Berry, E.A.,Huang, L.-S.,Zhang, Z.  et al.
(1999)  J.Bioenerg.Biomembr.  31 : 177 - 190

Mitochondrial cytochrome bc1 complex

Zhang, Z.,Berry, E.A.,Huang, L.-S.  et al.
(2000)  Subcell Biochem.  35 : 541 - 580

Physicochemical aspects of the movement of the Rieske iron sulfur protein during quinol oxidation by the bc1 complex from mitochondria and photosynthetic bacteria.

Crofts, A.R.,Hong, S.,Zhang, Z.  et al.
(1999)  Biochemistry  38 : 15827 - 15839

Reaction

Chain : C, P
UniProt : P18946 (CYB_CHICK)
Reaction : -
Cofactor: Evidence: Note:
heme b ECO:0000269 | PubMed:20025846
ECO:0000269 | PubMed:21575592
ECO:0000269 | PubMed:22690928
ECO:0000269 | PubMed:9565029
Binds 2 heme b groups non-covalently.
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
-
Cofactor: Evidence: Note:
[2Fe-2S] cluster ECO:0000255 | PROSITE-ProRule:PRU00628
Binds 1 [2Fe-2S] cluster per subunit. Fe-S cluster delivery to the Rieske protein is mediated by components of the iron sulfur (Fe-S) cluster assembly machinery that reside in the mitochondrial matrix (including HSC20 and LYRM7) (By similarity).