› 3a6z

X-ray diffraction
2.15Å resolution

Crystal structure of Pseudomonas sp. MIS38 lipase (PML) in the open conformation following dialysis against Ca-free buffer

Released:
DOI: 10.2210/pdb3a6z/pdb
PDB entry 3a6z coloured by chain, front view.
PDB entry 3a6z coloured by chain, side view.
PDB entry 3a6z coloured by chain, top view.
Source organism: Pseudomonas sp. MIS38
Primary publication:
X-ray crystallographic and MD simulation studies on the mechanism of interfacial activation of a family I.3 lipase with two lids.
Angkawidjaja C, Matsumura H, Koga Y, Takano K, Kanaya S
J Mol Biol 400 82-95 (2010)
PMID: 20438738

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193134 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipase Chains: A, C
Molecule details ›
Chains: A, C
Length: 617 amino acids
Theoretical weight: 64.56 KDa
Source organism: Pseudomonas sp. MIS38
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9RBY1 (Residues: 1-617; Coverage: 100%)
Sequence domains: RTX calcium-binding nonapeptide repeat (4 copies)
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand CA 17 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P6522
Unit cell:
a: 104.382Å b: 104.382Å c: 495.175Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.182 0.22
Expression system: Escherichia coli

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Citations

3 review citations

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