› 7cof

X-ray diffraction
1.08Å resolution

Cholesterol esterase from Burkholderia stabilis (orthorhombic crystal form)

Released:
DOI: 10.2210/pdb7cof/pdb
PDB entry 7cof coloured by chain, front view.
PDB entry 7cof coloured by chain, side view.
PDB entry 7cof coloured by chain, top view.
Source organism: Burkholderia stabilis
Primary publication:
Bacterial triacylglycerol lipase is a potential cholesterol esterase: Identification of a key determinant for sterol-binding specificity.
Yasutake Y, Konishi K, Muramatsu S, Yoshida K, Aburatani S, Sakasegawa SI, Tamura T
Int. J. Biol. Macromol. 167 578-586 (2021)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-103888 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AB hydrolase-1 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 320 amino acids
Theoretical weight: 33.24 KDa
Source organism: Burkholderia stabilis
UniProt:
  • Canonical: A0A1Y1BQV9 (Residues: 45-364; Coverage: 94%)
Gene name: BSFP_052170
Sequence domains: alpha/beta hydrolase fold

Ligands and Environments

4 bound ligands:
Ligand CA 1 x CA
Ligand GOL 2 x GOL
Ligand IMD 1 x IMD
Ligand IPA 2 x IPA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: C2221
Unit cell:
a: 58.241Å b: 61.365Å c: 147.177Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.099 0.098 0.118

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