1BCC

CYTOCHROME BC1 COMPLEX FROM CHICKEN


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.16 Å
  • R-Value Free: 0.310 
  • R-Value Work: 0.270 
  • R-Value Observed: 0.270 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.5 of the entry. See complete history



Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
UBIQUINOL CYTOCHROME C OXIDOREDUCTASE446Gallus gallusMutation(s): 0 
EC: 1.10.2.2
Membrane Entity: Yes 
UniProt
Find proteins for P31800 (Bos taurus)
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UniProt GroupP31800
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
UBIQUINOL CYTOCHROME C OXIDOREDUCTASE422Gallus gallusMutation(s): 0 
EC: 1.10.2.2
Membrane Entity: Yes 
UniProt
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UniProt GroupP23004
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
UBIQUINOL CYTOCHROME C OXIDOREDUCTASE380Gallus gallusMutation(s): 0 
EC: 1.10.2.2
Membrane Entity: Yes 
UniProt
Find proteins for P18946 (Gallus gallus)
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UniProt GroupP18946
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
UBIQUINOL CYTOCHROME C OXIDOREDUCTASE241Gallus gallusMutation(s): 0 
EC: 1.10.2.2
Membrane Entity: Yes 
UniProt
Find proteins for P00125 (Bos taurus)
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UniProt GroupP00125
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
UBIQUINOL CYTOCHROME C OXIDOREDUCTASE196Gallus gallusMutation(s): 0 
EC: 1.10.2.2
Membrane Entity: Yes 
UniProt
Find proteins for P13272 (Bos taurus)
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UniProt GroupP13272
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Entity ID: 6
MoleculeChains Sequence LengthOrganismDetailsImage
UBIQUINOL CYTOCHROME C OXIDOREDUCTASE109Gallus gallusMutation(s): 0 
EC: 1.10.2.2
Membrane Entity: Yes 
UniProt
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UniProt GroupP00129
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Entity ID: 7
MoleculeChains Sequence LengthOrganismDetailsImage
UBIQUINOL CYTOCHROME C OXIDOREDUCTASE81Gallus gallusMutation(s): 0 
EC: 1.10.2.2
Membrane Entity: Yes 
UniProt
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UniProt GroupP13271
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Entity ID: 8
MoleculeChains Sequence LengthOrganismDetailsImage
UBIQUINOL CYTOCHROME C OXIDOREDUCTASE78Gallus gallusMutation(s): 0 
EC: 1.10.2.2
Membrane Entity: Yes 
UniProt
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UniProt GroupP00126
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Entity ID: 9
MoleculeChains Sequence LengthOrganismDetailsImage
UBIQUINOL CYTOCHROME C OXIDOREDUCTASE33Gallus gallusMutation(s): 0 
EC: 1.10.2.2
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Entity ID: 10
MoleculeChains Sequence LengthOrganismDetailsImage
UBIQUINOL CYTOCHROME C OXIDOREDUCTASE62Gallus gallusMutation(s): 0 
EC: 1.10.2.2
Membrane Entity: Yes 
UniProt
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UniProt GroupP00130
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Small Molecules
Ligands 5 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
U10
Query on U10

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M [auth C]UBIQUINONE-10
C59 H90 O4
ACTIUHUUMQJHFO-UPTCCGCDSA-N
PEE
Query on PEE

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N [auth C],
R [auth E]
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine
C41 H78 N O8 P
MWRBNPKJOOWZPW-NYVOMTAGSA-N
HEM
Query on HEM

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K [auth C],
L [auth C],
P [auth D]
PROTOPORPHYRIN IX CONTAINING FE
C34 H32 Fe N4 O4
KABFMIBPWCXCRK-RGGAHWMASA-L
BOG
Query on BOG

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O [auth D]octyl beta-D-glucopyranoside
C14 H28 O6
HEGSGKPQLMEBJL-RKQHYHRCSA-N
FES
Query on FES

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Q [auth E]FE2/S2 (INORGANIC) CLUSTER
Fe2 S2
NIXDOXVAJZFRNF-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.16 Å
  • R-Value Free: 0.310 
  • R-Value Work: 0.270 
  • R-Value Observed: 0.270 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 169.59α = 90
b = 182.518β = 90
c = 240.573γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
MLPHAREphasing
RAVEmodel building
CNSrefinement
RAVEphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-08-19
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Non-polymer description, Version format compliance
  • Version 1.3: 2014-03-19
    Changes: Other
  • Version 1.4: 2014-10-29
    Changes: Non-polymer description
  • Version 1.5: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Advisory, Data collection, Database references, Derived calculations, Structure summary