› 5hc0

X-ray diffraction
1.4Å resolution

Structure of esterase Est22 with p-nitrophenol

Released:
DOI: 10.2210/pdb5hc0/pdb
PDB entry 5hc0 coloured by chain, front view.
PDB entry 5hc0 coloured by chain, side view.
PDB entry 5hc0 coloured by chain, top view.
Source organism: uncultured bacterium
Primary publication:
Structural insights of a hormone sensitive lipase homologue Est22.
Huang J, Huo YY, Ji R, Kuang S, Ji C, Xu XW, Li J
Sci Rep 6 28550 (2016)
PMID: 27328716

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124798 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha/beta hydrolase fold-3 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 365 amino acids
Theoretical weight: 39.08 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

3 bound ligands:
Ligand GOL 4 x GOL
Ligand NPO 2 x NPO
Ligand ACY 1 x ACY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: C2
Unit cell:
a: 121.823Å b: 57.22Å c: 54.578Å
α: 90° β: 97.46° γ: 90°
R-values:
R R work R free
0.133 0.132 0.158
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Metagenomics: novel enzymes from non-culturable microbes.
Berini et al. (2017)
18 other articles

4 mentions without citation

Structural insights of a hormone sensitive lipase homologue Est22.
Huang et al. (2016)
3 more