› 1ghp

X-ray diffraction
1.76Å resolution

STRUCTURES OF THE ACYL-ENZYME COMPLEX OF THE STAPHYLOCOCCUS AUREUS BETA-LACTAMASE MUTANT GLU166ASP:ASN170GLN WITH DEGRADED BENZYLPENICILLIN

Released:
DOI: 10.2210/pdb1ghp/pdb
PDB entry 1ghp coloured by chain, front view.
PDB entry 1ghp coloured by chain, side view.
PDB entry 1ghp coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Structures of the acyl-enzyme complexes of the Staphylococcus aureus beta-lactamase mutant Glu166Asp:Asn170Gln with benzylpenicillin and cephaloridine.
Chen CC, Herzberg O
Biochemistry 40 2351-8 (2001)
PMID: 11327855

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: 28.97 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

2 bound ligands:
Ligand SO4 4 x SO4
Ligand PNM 1 x PNM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: I222
Unit cell:
a: 52.9Å b: 89.7Å c: 138.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.185 0.264
Expression system: Escherichia coli

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Citations

2 review citations

Beta-lactamase inhibitors: evolving compounds for evolving resistance targets.
Georgopapadakou NH. (2004)
1 more

2 mentions without citation

Recognition of functional sites in protein structures.
Shulman-Peleg et al. (2004)
1 more