1BUL

6ALPHA-(HYDROXYPROPYL)PENICILLANATE ACYLATED ON NMC-A BETA-LACTAMASE FROM ENTEROBACTER CLOACAE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.89 Å
  • R-Value Free: 0.257 
  • R-Value Work: 0.209 
  • R-Value Observed: 0.209 

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Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Inhibition of the Nmc-A B-Lactamase by a Penicillanic Acid Derivative, and the Structural Bases for the Increase in Substrate Profile of This Antibiotic Resistance Enzyme

Mourey, L.Swaren, P.Miyashita, K.Bulychev, A.Mobashery, S.Samama, J.P.

(1998) J Am Chem Soc 120: 9382-9383


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
NMC-A BETA-LACTAMASE265Enterobacter cloacaeMutation(s): 0 
EC: 3.5.2.6
UniProt
Find proteins for P52663 (Enterobacter cloacae)
Explore P52663 
Go to UniProtKB:  P52663
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP52663
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.89 Å
  • R-Value Free: 0.257 
  • R-Value Work: 0.209 
  • R-Value Observed: 0.209 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 77.55α = 90
b = 52.46β = 90
c = 67.22γ = 90
Software Package:
Software NamePurpose
MOSFLMdata reduction
ROTAVATAdata reduction
AGROVATAdata reduction
AMoREphasing
X-PLORrefinement
CCP4data scaling
ROTAVATA)data scaling

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-12-30
    Type: Initial release
  • Version 1.1: 2008-03-03
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance