› 3s0z

X-ray diffraction
2.5Å resolution

Crystal structure of New Delhi Metallo-beta-lactamase (NDM-1)

Released:
DOI: 10.2210/pdb3s0z/pdb
PDB entry 3s0z coloured by chain, front view.
PDB entry 3s0z coloured by chain, side view.
PDB entry 3s0z coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
A structural view of the antibiotic degradation enzyme NDM-1 from a superbug.
Guo Y, Wang J, Niu G, Shui W, Sun Y, Zhou H, Zhang Y, Yang C, Lou Z, Rao Z
Protein Cell 2 384-94 (2011)
PMID: 21637961

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-122980 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallo-beta-lactamase type 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 224 amino acids
Theoretical weight: 23.58 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: E5KIY2 (Residues: 47-270; Coverage: 83%)
Gene names: AZ95_0035, BANRA_05542, E4K51_24975, ECS01_0033, G5603_25730, NDM1Dok01_N0175, RZR61_25285, bla NDM-1, blaNDM-1, pNDM102337_147, pNDM10505_149
Sequence domains: Metallo-beta-lactamase superfamily
Structure domains: Ribonuclease Z/Hydroxyacylglutathione hydrolase-like

Ligands and Environments

1 bound ligand:
Ligand ZN 4 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NE3A
Spacegroup: P31
Unit cell:
a: 40.696Å b: 40.696Å c: 215.292Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.236 0.234 0.267
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Metallo-ß-lactamases: a review.
Behzadi et al. (2020)
7 more

12 mentions without citation

Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.
Bahr et al. (2021)
11 more