› 5aob

X-ray diffraction
1.79Å resolution

The structure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis, Est2-butyrate bound

Released:
DOI: 10.2210/pdb5aob/pdb
PDB entry 5aob coloured by chain, front view.
PDB entry 5aob coloured by chain, side view.
PDB entry 5aob coloured by chain, top view.
Source organism: Thermogutta terrifontis
Primary publication:
The Structure of a Novel Thermophilic Esterase from the Planctomycetes Species, Thermogutta terrifontis Reveals an Open Active Site Due to a Minimal 'Cap' Domain.
Sayer C, Szabo Z, Isupov MN, Ingham C, Littlechild JA
Front Microbiol 6 1294 (2015)
PMID: 26635762

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102799 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
BD-FAE-like domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 286 amino acids
Theoretical weight: 31.56 KDa
Source organism: Thermogutta terrifontis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0X1KHD1 (Residues: 1-286; Coverage: 100%)
Sequence domains: BD-FAE
Structure domains: alpha/beta hydrolase

Ligands and Environments

5 bound ligands:
Ligand PG4 2 x PG4
Ligand BUA 1 x BUA
Ligand EDO 4 x EDO
Ligand CL 1 x CL
Ligand PEG 2 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P212121
Unit cell:
a: 61.684Å b: 70.578Å c: 75.305Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.176 0.221
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 citation in other articles

Polysaccharide utilization loci-driven enzyme discovery reveals BD-FAE: a bifunctional feruloyl and acetyl xylan esterase active on complex natural xylans.
Hameleers et al. (2021)
5 more

3 mentions without citation

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