5hc3

X-ray diffraction
2.4Å resolution

The structure of esterase Est22

Released:
Source organism: uncultured bacterium
Primary publication:
Structural insights of a hormone sensitive lipase homologue Est22.
Sci Rep 6 28550 (2016)
PMID: 27328716

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-124798 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha/beta hydrolase fold-3 domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 365 amino acids
Theoretical weight: 39.07 KDa
Source organism: uncultured bacterium
Expression system: Escherichia coli
UniProt:
  • Canonical: H6BDX1 (Residues: 1-344; Coverage: 100%)
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P212121
Unit cell:
a: 81.16Å b: 121.679Å c: 150.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.14 0.137 0.195
Expression system: Escherichia coli