› 3h17

X-ray diffraction
2.5Å resolution

Crystal structure of EstE5-PMSF (I)

Released:
DOI: 10.2210/pdb3h17/pdb
PDB entry 3h17 coloured by chain, front view.
PDB entry 3h17 coloured by chain, side view.
PDB entry 3h17 coloured by chain, top view.
Source organism: uncultured bacterium
Primary publication:
The crystal structure of an HSL-homolog EstE5 complex with PMSF reveals a unique configuration that inhibits the nucleophile Ser144 in catalytic triads.
Nam KH, Kim SJ, Priyadarshi A, Kim HS, Hwang KY
Biochem Biophys Res Commun 389 247-50 (2009)
PMID: 19715665

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-170934 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha/beta hydrolase fold-3 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 322 amino acids
Theoretical weight: 34.65 KDa
Source organism: uncultured bacterium
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q0GMU2 (Residues: 1-297; Coverage: 100%)
Gene name: estE5
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand PMS 1 x PMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 6C1
Spacegroup: P41212
Unit cell:
a: 61.137Å b: 61.137Å c: 148.919Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.187 0.235
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

12 citation in other articles

The metagenome-derived enzymes LipS and LipT increase the diversity of known lipases.
Chow et al. (2012)
11 more

3 mentions without citation

The grease trap: uncovering the mechanism of the hydrophobic lid in Cutibacterium acnes lipase.
Kim et al. (2020)
2 more