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› 1lhy

X-ray diffraction
2Å resolution

Crystal structure of TEM-30 beta-Lactamase at 2.0 Angstrom

Released:
DOI: 10.2210/pdb1lhy/pdb
Model geometry
Fit model/data
PDB entry 1lhy coloured by chain, front view.
PDB entry 1lhy coloured by chain, side view.
PDB entry 1lhy coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The structural bases of antibiotic resistance in the clinically derived mutant beta-lactamases TEM-30, TEM-32, and TEM-34.
Wang X, Minasov G, Shoichet BK
J Biol Chem 277 32149-56 (2002)
PMID: 12058046

Function and Biology Details

Reaction catalysed: 
a beta-lactam + H2O = 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-158652 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase TEM Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 28.87 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P62593 (Residues: 24-286; Coverage: 100%)
Gene names: bla, blaT-3, blaT-4, blaT-5, blaT-6
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: P212121
Unit cell:
a: 41.532Å b: 59.67Å c: 88.097Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 0.212
Expression system: Escherichia coli

Quick links

Citations

7 review citations

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

4 mentions without citation

Conserved water molecules stabilize the Omega-loop in class A beta-lactamases.
Bös et al. (2008)
3 more