6zl7

X-ray diffraction
1.5Å resolution

CRYSTAL STRUCTURE OF C173S MUTATION IN THE PMGL2 ESTERASE FROM PERMAFROST METAGENOMIC LIBRARY

Released:
Source organism: uncultured bacterium
Entry authors: Goryaynova DA, Boyko KM, Nikolaeva AY, Korzhenevskiy DA, Kryukova MV, Petrovskaya LE, Novototskaya-Vlasova KA, Rivkina EM, Dolgikh DA, Kirpichnikov MP, Popov VO

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: 351 amino acids
Theoretical weight: 37.55 KDa
Source organism: uncultured bacterium
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: 47.149Å b: 92.53Å c: 74.41Å
α: 90° β: 106.61° γ: 90°
R-values:
R R work R free
0.17 0.169 0.196
Expression system: Escherichia coli