› 1blc

X-ray diffraction
2.2Å resolution

INHIBITION OF BETA-LACTAMASE BY CLAVULANATE: TRAPPED INTERMEDIATES IN CRYOCRYSTALLOGRAPHIC STUDIES

Released:
DOI: 10.2210/pdb1blc/pdb
PDB entry 1blc coloured by chain, front view.
PDB entry 1blc coloured by chain, side view.
PDB entry 1blc coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Inhibition of beta-lactamase by clavulanate. Trapped intermediates in cryocrystallographic studies.
Chen CC, Herzberg O
J Mol Biol 224 1103-13 (1992)
PMID: 1569569

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133593 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 257 amino acids
Theoretical weight: 28.84 KDa
Source organism: Staphylococcus aureus
Expression system: Not provided
UniProt:
  • Canonical: P00807 (Residues: 25-281; Coverage: 100%)
Gene name: blaZ
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

3 bound ligands:
Ligand SO4 1 x SO4
Ligand CEM 1 x CEM
Ligand TEM 1 x TEM
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I222
Unit cell:
a: 54.1Å b: 88Å c: 141.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 not available not available
Expression system: Not provided

Quick links

Citations

15 review citations

Three decades of beta-lactamase inhibitors.
Drawz et al. (2010)
14 more

7 mentions without citation

Coupling between catalytic site and collective dynamics: a requirement for mechanochemical activity of enzymes.
Yang et al. (2005)
6 more