› 4p9n

X-ray diffraction
1.8Å resolution

Function and Biology Details

Reaction catalysed: 
A carboxylic ester + H(2)O = an alcohol + a carboxylate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177733 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha/beta hydrolase fold-3 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 304 amino acids
Theoretical weight: 33.46 KDa
Source organism: Saccharolobus shibatae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5NU42 (Residues: 2-305; Coverage: 100%)
Gene names: J5U21_01394, J5U22_01308, SshEstI
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: RIGAKU MICROMAX-007 HF
Spacegroup: I222
Unit cell:
a: 59.036Å b: 71.748Å c: 137.862Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.152 0.187
Expression system: Escherichia coli

Quick links

Citations

16 citation in other articles

Interdomain hydrophobic interactions modulate the thermostability of microbial esterases from the hormone-sensitive lipase family.
Li et al. (2015)
15 more

2 mentions without citation

Structural insights into the low pH adaptation of a unique carboxylesterase from Ferroplasma: altering the pH optima of two carboxylesterases.
Ohara et al. (2014)
1 more