› 1jkm

X-ray diffraction
1.85Å resolution

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

Released:
DOI: 10.2210/pdb1jkm/pdb
PDB entry 1jkm coloured by chain, front view.
PDB entry 1jkm coloured by chain, side view.
PDB entry 1jkm coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Crystal structure of brefeldin A esterase, a bacterial homolog of the mammalian hormone-sensitive lipase.
Wei Y, Contreras JA, Sheffield P, Osterlund T, Derewenda U, Kneusel RE, Matern U, Holm C, Derewenda ZS
Nat Struct Biol 6 340-5 (1999)
PMID: 10201402

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130634 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha/beta hydrolase fold-3 domain-containing protein 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: alpha/beta hydrolase

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

Quick links

Citations

9 review citations

Alpha/beta hydrolase fold enzymes: the family keeps growing.
Nardini et al. (1999)
8 more

21 mentions without citation

Carboxylic ester hydrolases from hyperthermophiles.
Levisson et al. (2009)
20 more