› 1btl

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE OF ESCHERICHIA COLI TEM1 BETA-LACTAMASE AT 1.8 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1btl/pdb
PDB entry 1btl coloured by chain, front view.
PDB entry 1btl coloured by chain, side view.
PDB entry 1btl coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution.
Jelsch C, Mourey L, Masson JM, Samama JP
Proteins 16 364-83 (1993)
PMID: 8356032

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-158652 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase TEM Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 28.98 KDa
Source organism: Escherichia coli
Expression system: Not provided
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 SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 43.1Å b: 64.4Å c: 91.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.164 not available
Expression system: Not provided

Quick links

Citations

18 review citations

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

76 mentions without citation

At the Interface of Chemical and Biological Synthesis: An Expanded Genetic Code.
Xiao et al. (2016)
75 more