PDBe 1ny0

X-ray diffraction
1.75Å resolution

Crystal Structure of the complex between M182T mutant of TEM-1 and a boronic acid inhibitor (NBF)

Released:
Source organism: Escherichia coli
Primary publication:
Recognition and resistance in TEM beta-lactamase.
Biochemistry 42 8434-44 (2003)
PMID: 12859188

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

Structure analysis Details

Assembly composition:
monomeric (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
UniProt:
  • Canonical: P62593 (Residues: 24-286; Coverage: 100%)
Gene names: bla, blaT-3, blaT-4, blaT-5, blaT-6
Sequence domains: Beta-lactamase enzyme family
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: P212121
Unit cell:
a: 41.289Å b: 58.967Å c: 88.63Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.171 0.198
Expression system: Escherichia coli