2ZC7

Crystal Structure of Class C beta-Lactamase ACT-1

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.247 
  • R-Value Work: 0.240 
  • R-Value Observed: 0.240 

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This is version 1.2 of the entry. See complete history. 


Literature

Structure of the plasmid-mediated class C beta-lactamase ACT-1

Shimizu-Ibuka, A., Bauvois, C., Sakai, H., Galleni, M.

(2008) Acta Crystallogr Sect F Struct Biol Cryst Commun 64: 334-337

  • DOI: https://doi.org/10.1107/S1744309108008531
  • Primary Citation of Related Structures:  
    2ZC7

  • PubMed Abstract: 

    The crystallographic structure of ACT-1, which is the first plasmid-mediated AmpC-type beta-lactamase to have been completely analyzed in terms of nucleotide sequence and which has a high degree of sequence similarity to the chromosomal AmpC enzymes of Enterobacter cloacae and the plasmid-encoded MIR-1, has been solved at 2.4 A resolution. The overall structure of ACT-1 is similar to those of other class C beta-lactamases, such as the AmpC enzymes from E. cloacae P99 and Escherichia coli.

    • Organizational Affiliation: 

    Department of Nutritional Science, Faculty of Applied Bio-Science, Tokyo University of Agriculture, Tokyo, Japan. a3shimizu@nodai.ac.jp


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-lactamase ACT-1
A, B, C, D
359Klebsiella pneumoniaeMutation(s): 0 
EC: 3.5.2.6
UniProt
Find proteins for Q48428 (Klebsiella pneumoniae)
Explore Q48428 
Go to UniProtKB:  Q48428
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ48428
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.247 
  • R-Value Work: 0.240 
  • R-Value Observed: 0.240 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 77.047α = 76.23
b = 80.521β = 68.88
c = 86.881γ = 63.46
Software Package:
Software NamePurpose
HKL-2000data collection
MOLREPphasing
CNSrefinement
HKL-2000data reduction
SCALEPACKdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-09-23
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-11-01
    Changes: Data collection, Database references, Refinement description