› 5olu

X-ray diffraction
1.8Å resolution

The crystal structure of a highly thermostable carboxyl esterase from Bacillus coagulans in complex with glycerol

Released:
DOI: 10.2210/pdb5olu/pdb
PDB entry 5olu coloured by chain, front view.
PDB entry 5olu coloured by chain, side view.
PDB entry 5olu coloured by chain, top view.
Source organism: Weizmannia coagulans DSM 1 = ATCC 7050
Primary publication:
A stereospecific carboxyl esterase from Bacillus coagulans hosting nonlipase activity within a lipase-like fold.
De Vitis V, Nakhnoukh C, Pinto A, Contente ML, Barbiroli A, Milani M, Bolognesi M, Molinari F, Gourlay LJ, Romano D
FEBS J 285 903-914 (2018)
PMID: 29278448

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-166059 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha/beta hydrolase family protein Chain: A
Molecule details ›
Chain: A
Length: 346 amino acids
Theoretical weight: 39.17 KDa
Source organism: Weizmannia coagulans DSM 1 = ATCC 7050
Expression system: Escherichia coli BL21(DE3)

Ligands and Environments

4 bound ligands:
Ligand GOL 3 x GOL
Ligand CL 8 x CL
Ligand PEG 1 x PEG
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P6322
Unit cell:
a: 137.644Å b: 137.644Å c: 83.636Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.149 0.148 0.169
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

The grease trap: uncovering the mechanism of the hydrophobic lid in Cutibacterium acnes lipase.
Kim et al. (2020)
1 more

1 mention without citation

A stereospecific carboxyl esterase from Bacillus coagulans hosting nonlipase activity within a lipase-like fold.
De Vitis et al. (2018)