› 1kge

X-ray diffraction
2Å resolution

STRUCTURE OF BETA-LACTAMASE ASN 170 MET MUTANT

Released:
DOI: 10.2210/pdb1kge/pdb
PDB entry 1kge coloured by chain, front view.
PDB entry 1kge coloured by chain, side view.
PDB entry 1kge coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Elimination of the hydrolytic water molecule in a class A beta-lactamase mutant: crystal structure and kinetics.
Zawadzke LE, Chen CC, Banerjee S, Li Z, Wäsch S, Kapadia G, Moult J, Herzberg O
Biochemistry 35 16475-82 (1996)
PMID: 8987980

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133592 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 258 amino acids
Theoretical weight: 28.99 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00807 (Residues: 25-281; Coverage: 100%)
Gene name: blaZ
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I222
Unit cell:
a: 54.3Å b: 94Å c: 139.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.156 not available
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Catalytic properties of class A beta-lactamases: efficiency and diversity.
Matagne et al. (1998)
2 more