4G3H

Crystal structure of helicobacter pylori arginase


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.230 
  • R-Value Work: 0.218 
  • R-Value Observed: 0.230 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structure and function studies on Helicobacter pylori arginase

Zhang, J.Zhang, X.Li, D.Hu, Y.Zou, Q.Wang, D.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Arginase (RocF)
A, B, C, D
330Helicobacter pylori 26695Mutation(s): 0 
Gene Names: HP_1399
UniProt
Find proteins for O25949 (Helicobacter pylori (strain ATCC 700392 / 26695))
Explore O25949 
Go to UniProtKB:  O25949
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO25949
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.230 
  • R-Value Work: 0.218 
  • R-Value Observed: 0.230 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 94.69α = 90
b = 102.24β = 90
c = 148.61γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
PHASESphasing
CNSrefinement
DENZOdata reduction
SCALAdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-08-01
    Type: Initial release
  • Version 1.1: 2014-12-17
    Changes: Data collection
  • Version 1.2: 2024-03-20
    Changes: Data collection, Database references, Derived calculations