› 4uhf

X-ray diffraction
1.08Å resolution

Structural studies of a thermophilic esterase from Thermogutta terrifontis (L37A mutant with butyrate bound)

Released:
DOI: 10.2210/pdb4uhf/pdb
PDB entry 4uhf coloured by chain, front view.
PDB entry 4uhf coloured by chain, side view.
PDB entry 4uhf 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-102434 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AB hydrolase-1 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 282 amino acids
Theoretical weight: 31.17 KDa
Source organism: Thermogutta terrifontis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0M3KKY6 (Residues: 1-282; Coverage: 100%)
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

3 bound ligands:
Ligand CAD 1 x CAD
Ligand BUA 3 x BUA
Ligand PGE 1 x PGE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P3221
Unit cell:
a: 43.23Å b: 43.23Å c: 227.83Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.115 0.114 0.136
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Enzymes from Extreme Environments and Their Industrial Applications.
Littlechild JA. (2015)
6 other articles

3 mentions without citation

Improving the 'tool box' for robust industrial enzymes.
Littlechild JA. (2017)
2 more