› 7cog

X-ray diffraction
2.1Å resolution

Cholesterol esterase from Burkholderia stabilis (monoclinic crystal form)

Released:
DOI: 10.2210/pdb7cog/pdb
PDB entry 7cog coloured by chain, front view.
PDB entry 7cog coloured by chain, side view.
PDB entry 7cog 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 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
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

1 bound ligand:
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NE3A
Spacegroup: P21
Unit cell:
a: 186.292Å b: 47.092Å c: 70.082Å
α: 90° β: 90.05° γ: 90°
R-values:
R R work R free
0.237 0.219 0.252

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