› 4mez

X-ray diffraction
2.05Å resolution

Crystal structure of M68L/M69T double mutant TEM-1

Released:
DOI: 10.2210/pdb4mez/pdb
PDB entry 4mez coloured by chain, front view.
PDB entry 4mez coloured by chain, side view.
PDB entry 4mez coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The Structural Dynamics of Engineered β-Lactamases Vary Broadly on Three Timescales yet Sustain Native Function.
Gobeil SMC, Ebert MCCJC, Park J, Gagné D, Doucet N, Berghuis AM, Pleiss J, Pelletier JN
Sci Rep 9 6656 (2019)
PMID: 31040324

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 263 amino acids
Theoretical weight: 28.89 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

3 bound ligands:
Ligand CL 2 x CL
Ligand SO4 3 x SO4
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P1
Unit cell:
a: 34.333Å b: 55.071Å c: 77.681Å
α: 70.83° β: 81.22° γ: 71.84°
R-values:
R R work R free
0.195 0.192 0.248
Expression system: Escherichia coli

Quick links

Citations

1 review citation

A mechanistic view of enzyme evolution.
Yang et al. (2020)
9 other articles

2 mentions without citation

The Structural Dynamics of Engineered β-Lactamases Vary Broadly on Three Timescales yet Sustain Native Function.
Gobeil et al. (2019)
1 more