› 4uhd

X-ray diffraction
1.07Å resolution

Structural studies of a thermophilic esterase from Thermogutta terrifontis (acetate bound)

Released:
DOI: 10.2210/pdb4uhd/pdb
PDB entry 4uhd coloured by chain, front view.
PDB entry 4uhd coloured by chain, side view.
PDB entry 4uhd 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
UniProt:
  • Canonical: A0A0M3KKY6 (Residues: 1-282; Coverage: 100%)
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

4 bound ligands:
Ligand CL 1 x CL
Ligand MG 1 x MG
Ligand ACT 2 x ACT
Ligand PEG 2 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P3221
Unit cell:
a: 43.28Å b: 43.28Å c: 227.29Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.094 0.094 0.112
Expression system: Escherichia coli

Quick links

Citations

1 review citation

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

2 mentions without citation

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