› 4ftw

X-ray diffraction
2.3Å resolution

Crystal structure of a carboxyl esterase N110C/L145H at 2.3 angstrom resolution

Released:
DOI: 10.2210/pdb4ftw/pdb
PDB entry 4ftw coloured by chain, front view.
PDB entry 4ftw coloured by chain, side view.
PDB entry 4ftw coloured by chain, top view.
Source organism: Cereibacter sphaeroides 2.4.1
Primary publication:
Enhanced enantioselectivity of a carboxyl esterase from Rhodobacter sphaeroides by directed evolution.
Ma J, Wu L, Guo F, Gu J, Tang X, Jiang L, Liu J, Zhou J, Yu H
Appl Microbiol Biotechnol 97 4897-906 (2013)
PMID: 22987200

Function and Biology Details

Reaction catalysed: 
A carboxylic ester + H(2)O = an alcohol + a carboxylate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174607 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospholipase/carboxylesterase/thioesterase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 285 amino acids
Theoretical weight: 29.92 KDa
Source organism: Cereibacter sphaeroides 2.4.1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q3J2V1 (Residues: 1-220; Coverage: 100%)
Gene name: RSP_2728
Sequence domains: Phospholipase/Carboxylesterase
Structure domains: alpha/beta hydrolase

Ligands and Environments

4 bound ligands:
Ligand PIN 1 x PIN
Ligand 3CM 1 x 3CM
Ligand NA 1 x NA
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P3121
Unit cell:
a: 112.382Å b: 112.382Å c: 47.569Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.242 0.239 0.299
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Computational tools for the evaluation of laboratory-engineered biocatalysts.
Romero-Rivera et al. (2016)
1 more

1 mention without citation

Thioesterase enzyme families: Functions, structures, and mechanisms.
Caswell et al. (2022)