5F1G

Crystal structure of AmpC BER adenylylated in the cytoplasm

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.76 Å
  • R-Value Free: 0.192 
  • R-Value Work: 0.172 
  • R-Value Observed: 0.173 

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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
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-lactamase366Escherichia coliMutation(s): 0 
Gene Names: ampC
EC: 3.5.2.6
UniProt
Find proteins for A7TUE6 (Escherichia coli)
Explore A7TUE6 
Go to UniProtKB:  A7TUE6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA7TUE6
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.76 Å
  • R-Value Free: 0.192 
  • R-Value Work: 0.172 
  • R-Value Observed: 0.173 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 60.478α = 90
b = 65.414β = 90
c = 106.115γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data processing
HKL-2000data scaling
Cootmodel building

Structure Validation

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Ligand Structure Quality Assessment 


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Entry History & Funding Information

Deposition Data

Funding OrganizationLocationGrant Number
National Research Foundation of KoreaKorea, Republic OfNRF-2015R 1A2A2A 01004168
National Research Foundation of KoreaKorea, Republic OfNRF-2015M 1A5A 1037480
KIOST in-house programsKorea, Republic OfPE99314
KIOST in-house programsKorea, Republic OfPE99302

Revision History  (Full details and data files)

  • Version 1.0: 2016-12-07
    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