› 4id4

X-ray diffraction
1.05Å resolution

Crystal structure of chimeric beta-lactamase cTEM-17m

Released:
DOI: 10.2210/pdb4id4/pdb
PDB entry 4id4 coloured by chain, front view.
PDB entry 4id4 coloured by chain, side view.
PDB entry 4id4 coloured by chain, top view.
Source organisms:
Primary publication:
Maintenance of native-like protein dynamics may not be required for engineering functional proteins.
Gobeil SMC, Clouthier CM, Park J, Gagné D, Berghuis AM, Doucet N, Pelletier JN
Chem Biol 21 1330-1340 (2014)
PMID: 25200606

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-147842 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase PSE-4; Beta-lactamase TEM Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 28.88 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P62593 (Residues: 24-147, 189-286; Coverage: 84%)
  • Canonical: P16897 (Residues: 145-185; Coverage: 15%)
Gene names: bla, blaT-3, blaT-4, blaT-5, blaT-6, carB1, pse4
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

2 bound ligands:
Ligand CL 5 x CL
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P212121
Unit cell:
a: 36.73Å b: 58.72Å c: 109.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.116 0.115 0.138
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Perspective: Defining and quantifying the role of dynamics in enzyme catalysis.
Warshel et al. (2016)
4 more

4 mentions without citation

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