› 4c01

X-ray diffraction
2.3Å resolution

Complete crystal structure of carboxylesterase Cest-2923 (lp_2923) from Lactobacillus plantarum WCFS1

Released:
DOI: 10.2210/pdb4c01/pdb
PDB entry 4c01 coloured by chain, front view.
PDB entry 4c01 coloured by chain, side view.
PDB entry 4c01 coloured by chain, top view.
Source organism: Lactiplantibacillus plantarum WCFS1
Primary publication:
Structure, biochemical characterization and analysis of the pleomorphism of carboxylesterase Cest-2923 from Lactobacillus plantarum WCFS1.
Benavente R, Esteban-Torres M, Acebrón I, de Las Rivas B, Muñoz R, Alvarez Y, Mancheño JM
FEBS J 280 6658-71 (2013)
PMID: 24127688

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123793 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
BD-FAE-like domain-containing protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 282 amino acids
Theoretical weight: 31.28 KDa
Source organism: Lactiplantibacillus plantarum WCFS1
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: F9US10 (Residues: 1-276; Coverage: 100%)
Gene name: lp_2923
Sequence domains: BD-FAE
Structure domains: alpha/beta hydrolase

Ligands and Environments

4 bound ligands:
Ligand ACT 6 x ACT
Ligand SO4 8 x SO4
Ligand QY9 5 x QY9
Ligand CCN 12 x CCN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: C2
Unit cell:
a: 244.886Å b: 141.385Å c: 82.695Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.225 0.279
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

An Overview into Polyethylene Terephthalate (PET) Hydrolases and Efforts in Tailoring Enzymes for Improved Plastic Degradation.
Khairul Anuar et al. (2022)
14 other articles

1 mention without citation

The Structure of a Novel Thermophilic Esterase from the Planctomycetes Species, Thermogutta terrifontis Reveals an Open Active Site Due to a Minimal 'Cap' Domain.
Sayer et al. (2015)