› 7b4q

X-ray diffraction
1.61Å resolution

Structure of a cold active HSL family esterase reveals mechanisms of low temperature adaptation and substrate specificity

Released:
DOI: 10.2210/pdb7b4q/pdb
PDB entry 7b4q coloured by chain, front view.
PDB entry 7b4q coloured by chain, side view.
PDB entry 7b4q coloured by chain, top view.
Source organism: Sutcliffiella cohnii NBRC 15565
Primary publication:
Structure and in silico simulations of a cold-active esterase reveals its prime cold-adaptation mechanism.
Noby N, Auhim HS, Winter S, Worthy HL, Embaby AM, Saeed H, Hussein A, Pudney CR, Rizkallah PJ, Wells SA, Jones DD
OpenAccess logo Open Biol 11 210182 (2021)
PMID: 34847772

Function and Biology Details

Reaction catalysed: 
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-104321 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha/beta hydrolase fold-3 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 320 amino acids
Theoretical weight: 35.53 KDa
Source organism: Sutcliffiella cohnii NBRC 15565
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A2K9UV39 (Residues: 1-320; Coverage: 100%)
Sequence domains: alpha/beta hydrolase fold

Ligands and Environments

4 bound ligands:
Ligand EDO 4 x EDO
Ligand GOL 1 x GOL
Ligand PEG 1 x PEG
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P43212
Unit cell:
a: 109.883Å b: 109.883Å c: 126.772Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.167 0.193
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Cold-Active Lipases and Esterases: A Review on Recombinant Overexpression and Other Essential Issues.
Matinja et al. (2022)
1 more

2 mentions without citation

Structure and in silico simulations of a cold-active esterase reveals its prime cold-adaptation mechanism.
Noby et al. (2021)
1 more