1XMP

Crystal Structure of PurE (BA0288) from Bacillus anthracis at 1.8 Resolution


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.205 
  • R-Value Work: 0.167 
  • R-Value Observed: 0.169 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Crystal structure of PurE (BA0288) from Bacillus anthracis at 1.8 A resolution

Boyle, M.P.Kalliomaa, A.K.Levdikov, V.Blagova, E.Fogg, M.J.Brannigan, J.A.Wilson, K.S.Wilkinson, A.J.

(2005) Proteins 61: 674-676


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
phosphoribosylaminoimidazole carboxylase
A, B, C, D, E
A, B, C, D, E, F, G, H
170Bacillus anthracisMutation(s): 0 
Gene Names: purE
EC: 4.1.1.21
UniProt
Find proteins for A0A6L7HA71 (Bacillus anthracis)
Explore A0A6L7HA71 
Go to UniProtKB:  A0A6L7HA71
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A6L7HA71
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.205 
  • R-Value Work: 0.167 
  • R-Value Observed: 0.169 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 168.263α = 90
b = 76.484β = 96.68
c = 102.675γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data reduction
SCALEPACKdata scaling
MOLREPphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-11-16
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-08-23
    Changes: Data collection, Database references, Refinement description