6qin

X-ray diffraction
1.6Å resolution

CRYSTAL STRUCTURE OF THE PMGL2 ESTERASE FROM PERMAFROST METAGENOMIC LIBRARY

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-103008 (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: 349 amino acids
Theoretical weight: 37.32 KDa
Source organism: permafrost metagenome
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A142J6I6 (Residues: 1-343; Coverage: 100%)
Sequence domains: alpha/beta hydrolase fold

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P21
Unit cell:
a: 47.01Å b: 92.35Å c: 74.23Å
α: 90° β: 106.83° γ: 90°
R-values:
R R work R free
0.158 0.157 0.187
Expression system: Escherichia coli