› 1tem

X-ray diffraction
1.95Å resolution

6 ALPHA HYDROXYMETHYL PENICILLOIC ACID ACYLATED ON THE TEM-1 BETA-LACTAMASE FROM ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb1tem/pdb
PDB entry 1tem coloured by chain, front view.
PDB entry 1tem coloured by chain, side view.
PDB entry 1tem coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal Structure of 6Alpha-Hydroxymethylpenicillanate Complexed to the Tem-1 Beta-Lactamase from Escherichia Coli: Evidence on the Mechanism of Action of a Novel Inhibitor Designed by a Computer-Aided Process
Maveyraud L, Massova I, Birck C, Miyashita K, Samama JP, Mobashery S
J. Am. Chem. Soc. 118 7435- (1996)

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: 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 ALP 1 x ALP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: P212121
Unit cell:
a: 42.1Å b: 63.1Å c: 88.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.156 0.202
Expression system: Escherichia coli

Quick links

Citations

4 mentions without citation

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