› 1e25

X-ray diffraction
1.9Å resolution

The high resolution structure of PER-1 class A beta-lactamase

Released:
DOI: 10.2210/pdb1e25/pdb
PDB entry 1e25 coloured by chain, front view.
PDB entry 1e25 coloured by chain, side view.
PDB entry 1e25 coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
The high resolution crystal structure for class A beta-lactamase PER-1 reveals the bases for its increase in breadth of activity.
Tranier S, Bouthors AT, Maveyraud L, Guillet V, Sougakoff W, Samama JP
J Biol Chem 275 28075-82 (2000)
PMID: 10825176

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-153390 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Extended-spectrum beta-lactamase PER-1 Chain: A
Molecule details ›
Chain: A
Length: 282 amino acids
Theoretical weight: 30.95 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: P37321 (Residues: 27-308; Coverage: 100%)
Gene name: per1
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE DW32
Spacegroup: P43
Unit cell:
a: 84.6Å b: 84.6Å c: 46.89Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.14 0.14 0.183
Expression system: Escherichia coli

Quick links

Citations

6 review citations

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

13 mentions without citation

Analysis of the plasticity of location of the Arg244 positive charge within the active site of the TEM-1 beta-lactamase.
Marciano et al. (2009)
12 more