› 4ivi

X-ray diffraction
2Å resolution

Crystal structure of a family VIII carboxylesterase.

Released:
DOI: 10.2210/pdb4ivi/pdb
PDB entry 4ivi coloured by chain, front view.
PDB entry 4ivi coloured by chain, side view.
PDB entry 4ivi coloured by chain, top view.
Source organism: uncultured bacterium
Primary publication:
Structural basis for the β-lactamase activity of EstU1, a family VIII carboxylesterase.
Cha SS, An YJ, Jeong CS, Kim MK, Jeon JH, Lee CM, Lee HS, Kang SG, Lee JH
Proteins 81 2045-51 (2013)
PMID: 23737193

Function and Biology Details

Reaction catalysed: 
A carboxylic ester + H(2)O = an alcohol + a carboxylate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
homo octamer
Assembly name:
PDBe Complex ID:
PDB-CPX-125528 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase-related domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 434 amino acids
Theoretical weight: 48.25 KDa
Source organism: uncultured bacterium
UniProt:
  • Canonical: K4HQE7 (Residues: 1-426; Coverage: 100%)
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
1 modified residue:
Ligand MSE 18 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: I422
Unit cell:
a: 149.065Å b: 149.065Å c: 171.131Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.182 0.198

Quick links

Citations

1 review citation

Class C β-Lactamases: Molecular Characteristics.
Philippon et al. (2022)
15 other articles

3 mentions without citation

Discovery and Design of Family VIII Carboxylesterases as Highly Efficient Acyltransferases.
Müller et al. (2021)
2 more