1OAC

CRYSTAL STRUCTURE OF A QUINOENZYME: COPPER AMINE OXIDASE OF ESCHERICHIA COLI AT 2 ANGSTROEMS RESOLUTION


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Observed: 0.162 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution.

Parsons, M.R.Convery, M.A.Wilmot, C.M.Yadav, K.D.Blakeley, V.Corner, A.S.Phillips, S.E.McPherson, M.J.Knowles, P.F.

(1995) Structure 3: 1171-1184

  • DOI: https://doi.org/10.1016/s0969-2126(01)00253-2
  • Primary Citation of Related Structures:  
    1OAC

  • PubMed Abstract: 

    Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyze the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ).


  • Organizational Affiliation

    Department of Biochemistry and Molecular Biology, University of Leeds, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
COPPER AMINE OXIDASE
A, B
727Escherichia coliMutation(s): 0 
EC: 1.4.3.6
UniProt
Find proteins for P46883 (Escherichia coli (strain K12))
Explore P46883 
Go to UniProtKB:  P46883
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP46883
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Observed: 0.162 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 135.732α = 90
b = 167.775β = 90
c = 81.904γ = 90
Software Package:
Software NamePurpose
MOSFLMdata reduction
PROLSQrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1996-04-03
    Type: Initial release
  • Version 1.1: 2008-03-03
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance