4rl0

X-ray diffraction
1.3Å resolution

Structural and mechanistic insights into NDM-1 catalyzed hydrolysis of cephalosporins

Released:
Source organism: Klebsiella pneumoniae
Entry authors: Feng H, Ding J, Zhu D, Liu X, Xu X, Zhang Y, Zang S, Wang D-C, Liu W

Function and Biology Details

Reaction catalysed:
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallo-beta-lactamase type 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 242 amino acids
Theoretical weight: 25.63 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: C7C422 (Residues: 29-270; Coverage: 100%)
Gene name: blaNDM-1
Sequence domains: Metallo-beta-lactamase superfamily
Structure domains: Ribonuclease Z/Hydroxyacylglutathione hydrolase-like

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 39.18Å b: 78.89Å c: 133.06Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.134 0.131 0.157
Expression system: Escherichia coli