› 1ome

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF THE OMEGA LOOP DELETION MUTANT (RESIDUES 163-178 DELETED) OF BETA-LACTAMASE FROM STAPHYLOCOCCUS AUREUS PC1

Released:
DOI: 10.2210/pdb1ome/pdb
PDB entry 1ome coloured by chain, front view.
PDB entry 1ome coloured by chain, side view.
PDB entry 1ome coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Role of the omega-loop in the activity, substrate specificity, and structure of class A beta-lactamase.
Banerjee S, Pieper U, Kapadia G, Pannell LK, Herzberg O
Biochemistry 37 3286-96 (1998)
PMID: 9521648

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 Chains: A, B
Molecule details ›
Chains: A, B
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

1 bound ligand:
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: P21
Unit cell:
a: 76Å b: 55Å c: 79.2Å
α: 90° β: 90.25° γ: 90°
R-values:
R R work R free
0.19 0.19 0.298
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Resistance to Novel β-Lactam-β-Lactamase Inhibitor Combinations: The "Price of Progress".
Papp-Wallace et al. (2020)
5 more

4 mentions without citation

Update on LIPID MAPS classification, nomenclature, and shorthand notation for MS-derived lipid structures.
Liebisch et al. (2020)
3 more