› 5ah0

X-ray diffraction
2.5Å resolution

STRUCTURE OF LIPASE 1 FROM PELOSINUS FERMENTANS

Released:
DOI: 10.2210/pdb5ah0/pdb
PDB entry 5ah0 coloured by chain, front view.
PDB entry 5ah0 coloured by chain, side view.
PDB entry 5ah0 coloured by chain, top view.
Source organism: Pelosinus fermentans DSM 17108
Primary publication:
Characterization of a poly(butylene adipate-co-terephthalate)- hydrolyzing lipase from Pelosinus fermentans.
Biundo A, Hromic A, Pavkov-Keller T, Gruber K, Quartinello F, Haernvall K, Perz V, Arrell MS, Zinn M, Ribitsch D, Guebitz GM
Appl Microbiol Biotechnol 100 1753-1764 (2016)
PMID: 26490551

Function and Biology Details

Reaction catalysed: 
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-100798 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
triacylglycerol lipase Chains: A, B
Molecule details ›
Chains: A, B
Length: 387 amino acids
Theoretical weight: 42.9 KDa
Source organism: Pelosinus fermentans DSM 17108
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0A0YMQ9 (Residues: 2-387; Coverage: 99%)
Gene name: pfl1
Structure domains: alpha/beta hydrolase

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand PEG 2 x PEG
Ligand K 1 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P41212
Unit cell:
a: 91.8Å b: 91.8Å c: 215.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.194 0.243
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Bacterial lipases: A review on purification and characterization.
Javed et al. (2018)
3 more

1 mention without citation

Bacillus sp. JR3 esterase LipJ: A new mesophilic enzyme showing traces of a thermophilic past.
Ribera et al. (2017)