5GZW

Crystal structure of AmpC BER adenylylated by acetyl-AMP

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.49 Å
  • R-Value Free: 0.237 
  • R-Value Work: 0.211 
  • R-Value Observed: 0.212 

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Literature

Structural and mechanistic insights into the inhibition of class C beta-lactamases through the adenylylation of the nucleophilic serine.

Kim, M.K., An, Y.J., Na, J.H., Seol, J.H., Ryu, J.Y., Lee, J.W., Kang, L.W., Chung, K.M., Lee, J.H., Moon, J.H., Lee, J.S., Cha, S.S.

(2017) J Antimicrob Chemother 72: 735-743

  • DOI: https://doi.org/10.1093/jac/dkw491
  • Primary Citation of Related Structures:  
    5F1F, 5F1G, 5GZW

  • PubMed Abstract: 

    : Investigation into the adenylylation of the nucleophilic serine in AmpC BER and CMY-10 extended-spectrum class C β-lactamases.

    • Organizational Affiliation: 

    Marine Biotechnology Research Center, Korea Institute of Ocean Science and Technology (KIOST), Ansan, 15627, Republic of Korea.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-lactamase
A, B
366Escherichia coliMutation(s): 0 
Gene Names: ampC
EC: 3.5.2.6
UniProt
Find proteins for A0A076YIY5 (Escherichia coli)
Explore A0A076YIY5 
Go to UniProtKB:  A0A076YIY5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A076YIY5
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.49 Å
  • R-Value Free: 0.237 
  • R-Value Work: 0.211 
  • R-Value Observed: 0.212 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 61.48α = 90
b = 65.039β = 90
c = 177.271γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data processing
HKL-2000data scaling

Structure Validation

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Entry History & Funding Information

Deposition Data

Funding OrganizationLocationGrant Number
Korea, Republic Of--

Revision History  (Full details and data files)

  • Version 1.0: 2017-10-11
    Type: Initial release
  • Version 1.1: 2021-03-31
    Changes: Database references, Structure summary
  • Version 1.2: 2023-11-08
    Changes: Data collection, Database references, Refinement description