› 3o0d

X-ray diffraction
1.7Å resolution

Crystal structure of Lip2 lipase from Yarrowia lipolytica at 1.7 A resolution

Released:
DOI: 10.2210/pdb3o0d/pdb
PDB entry 3o0d coloured by chain, front view.
PDB entry 3o0d coloured by chain, side view.
PDB entry 3o0d coloured by chain, top view.
Source organism: Yarrowia lipolytica
Primary publication:
Exploring the conformational states and rearrangements of Yarrowia lipolytica Lipase.
Bordes F, Barbe S, Escalier P, Mourey L, André I, Marty A, Tranier S
Biophys J 99 2225-34 (2010)
PMID: 20923657

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192869 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
triacylglycerol lipase Chains: A, B, C, D, E, F, G
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 301 amino acids
Theoretical weight: 33.42 KDa
Source organism: Yarrowia lipolytica
Expression system: Yarrowia lipolytica
UniProt:
  • Canonical: Q9P8F7 (Residues: 34-334; Coverage: 98%)
Gene names: B0I71DRAFT_136010, Lip2, YALI1_A21372g, lip2
Sequence domains:
Structure domains: alpha/beta hydrolase

Ligands and Environments

4 bound ligands:
Ligand NAG 14 x NAG
Ligand MPD 13 x MPD
Ligand MRD 4 x MRD
Ligand K 7 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 115.354Å b: 132.141Å c: 137.255Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.171 0.211
Expression system: Yarrowia lipolytica

Quick links

Citations

5 review citations

The Lid Domain in Lipases: Structural and Functional Determinant of Enzymatic Properties.
Khan et al. (2017)
4 more

6 mentions without citation

Recent Advances in the Enzymatic Synthesis of Polyester.
Wang et al. (2022)
5 more