› 1nyy

X-ray diffraction
1.9Å resolution

Crystal Structure of the complex between M182T mutant of TEM-1 and a boronic acid inhibitor (105)

Released:
DOI: 10.2210/pdb1nyy/pdb
PDB entry 1nyy coloured by chain, front view.
PDB entry 1nyy coloured by chain, side view.
PDB entry 1nyy coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Recognition and resistance in TEM beta-lactamase.
Wang X, Minasov G, Blázquez J, Caselli E, Prati F, Shoichet BK
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
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: 28.91 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:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand 105 1 x 105
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: P212121
Unit cell:
a: 41.498Å b: 61.953Å c: 89.065Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 0.23
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

1 mention without citation

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