› 1esd

X-ray diffraction
2.3Å resolution

THE MOLECULAR MECHANISM OF ENANTIORECOGNITION BY ESTERASES

Released:
DOI: 10.2210/pdb1esd/pdb
PDB entry 1esd coloured by chain, front view.
PDB entry 1esd coloured by chain, side view.
PDB entry 1esd coloured by chain, top view.
Source organism: Streptomyces scabiei
Primary publication:
A novel variant of the catalytic triad in the Streptomyces scabies esterase.
Wei Y, Schottel JL, Derewenda U, Swenson L, Patkar S, Derewenda ZS
Nat Struct Biol 2 218-23 (1995)
PMID: 7773790

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149567 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Esterase Chain: A
Molecule details ›
Chain: A
Length: 306 amino acids
Theoretical weight: 33 KDa
Source organism: Streptomyces scabiei
UniProt:
  • Canonical: P22266 (Residues: 40-345; Coverage: 100%)
Gene name: estA
Sequence domains: GDSL-like Lipase/Acylhydrolase family
Structure domains: SGNH hydrolase

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 131.133Å b: 48.596Å c: 70.353Å
α: 90° β: 118.03° γ: 90°
R-values:
R R work R free
0.18 not available not available

Quick links

Citations

11 review citations

Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases.
Jaeger et al. (1999)
10 more

3 mentions without citation

Carboxylic ester hydrolases: Classification and database derived from their primary, secondary, and tertiary structures.
Chen et al. (2016)
2 more