5E2G

Crystal Structure of D-alanine Carboxypeptidase AmpC from Burkholderia cenocepacia


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.65 Å
  • R-Value Free: 0.189 
  • R-Value Work: 0.150 
  • R-Value Observed: 0.153 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

Crystal Structure of D-alanine Carboxypeptidase AmpC from Burkholderia cenocepacia

Kim, Y.Joachimiak, G.Endres, M.Babnigg, G.Joachimiak, A.Midwest Center for Structural Genomics (MCSG)

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-lactamase
A, B
361Burkholderia cenocepacia J2315Mutation(s): 0 
Gene Names: ampCBCAS0156
EC: 3.5.2.6
UniProt
Find proteins for B4EPS2 (Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610))
Explore B4EPS2 
Go to UniProtKB:  B4EPS2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupB4EPS2
Sequence Annotations
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  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.65 Å
  • R-Value Free: 0.189 
  • R-Value Work: 0.150 
  • R-Value Observed: 0.153 
  • Space Group: P 32
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 85.965α = 90
b = 85.965β = 90
c = 90.399γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-3000data reduction
HKL-3000data scaling
HKL-3000phasing
SBC-Collectdata collection

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-10-14
    Type: Initial release