5mmd

X-ray diffraction
1.75Å resolution

TMB-1. Structural insights into TMB-1 and the role of residue 119 and 228 in substrate and inhibitor binding

Released:

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

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-197507 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallo-beta-lactamase type 2 Chains: E, F
Molecule details ›
Chains: E, F
Length: 229 amino acids
Theoretical weight: 25.2 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: T2HNV0 (Residues: 18-245; Coverage: 100%)
Gene name: blaTMB-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: BESSY BEAMLINE 14.1
Spacegroup: P21212
Unit cell:
a: 71.398Å b: 127.195Å c: 44.274Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.192 0.248
Expression system: Escherichia coli BL21(DE3)