PDBe 1jkm

X-ray diffraction
1.85Å resolution

BREFELDIN A ESTERASE, A BACTERIAL HOMOLOGUE OF HUMAN HORMONE SENSITIVE LIPASE

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Brefeldin A esterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 361 amino acids
Theoretical weight: 38.56 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: O68884 (Residues: 10-370; Coverage: 97%)
Sequence domains: alpha/beta hydrolase fold
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: C2
Unit cell:
a: 140.7Å b: 82.6Å c: 81.5Å
α: 90° β: 112.5° γ: 90°
R-values:
R R work R free
0.17 0.169 0.206
Expression system: Escherichia coli