› 1yt4

X-ray diffraction
1.4Å resolution

Crystal structure of TEM-76 beta-lactamase at 1.4 Angstrom resolution

Released:
DOI: 10.2210/pdb1yt4/pdb
PDB entry 1yt4 coloured by chain, front view.
PDB entry 1yt4 coloured by chain, side view.
PDB entry 1yt4 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural consequences of the inhibitor-resistant Ser130Gly substitution in TEM beta-lactamase.
Thomas VL, Golemi-Kotra D, Kim C, Vakulenko SB, Mobashery S, Shoichet BK
Biochemistry 44 9330-8 (2005)
PMID: 15981999

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 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: 28.91 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P212121
Unit cell:
a: 41.601Å b: 59.707Å c: 88.36Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 0.223
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Natural evolution of TEM-1 β-lactamase: experimental reconstruction and clinical relevance.
Salverda et al. (2010)
4 more

7 mentions without citation

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