› 4uhh

X-ray diffraction
1.06Å resolution

Structural studies of a thermophilic esterase from Thermogutta terrifontis (cacodylate complex)

Released:
DOI: 10.2210/pdb4uhh/pdb
PDB entry 4uhh coloured by chain, front view.
PDB entry 4uhh coloured by chain, side view.
PDB entry 4uhh coloured by chain, top view.
Source organism: Thermogutta terrifontis
Primary publication:
Structural studies of a thermophilic esterase from a new Planctomycetes species, Thermogutta terrifontis.
Sayer C, Isupov MN, Bonch-Osmolovskaya E, Littlechild JA
FEBS J 282 2846-57 (2015)
PMID: 26011036

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102190 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AB hydrolase-1 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 274 amino acids
Theoretical weight: 30.22 KDa
Source organism: Thermogutta terrifontis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0H4B872 (Residues: 1-274; Coverage: 100%)
Gene name: THTE_1476
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

3 bound ligands:
Ligand CAD 1 x CAD
Ligand PEG 1 x PEG
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P3221
Unit cell:
a: 43.31Å b: 43.31Å c: 226.85Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.104 0.103 0.123
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Enzymes from Extreme Environments and Their Industrial Applications.
Littlechild JA. (2015)
1 more

2 mentions without citation

Innovation and tinkering in the evolution of oxidases.
Jabłońska et al. (2022)
1 more