› 3icv

X-ray diffraction
1.49Å resolution

Structural Consequences of a Circular Permutation on Lipase B from Candida Antartica

Released:
DOI: 10.2210/pdb3icv/pdb
PDB entry 3icv coloured by chain, front view.
PDB entry 3icv coloured by chain, side view.
PDB entry 3icv coloured by chain, top view.
Source organism: Moesziomyces antarcticus
Primary publication:
Structural redesign of lipase B from Candida antarctica by circular permutation and incremental truncation.
Qian Z, Horton JR, Cheng X, Lutz S
J Mol Biol 393 191-201 (2009)
PMID: 19683009

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154387 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipase B Chain: A
Molecule details ›
Chain: A
Length: 316 amino acids
Theoretical weight: 32.9 KDa
Source organism: Moesziomyces antarcticus
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P41365 (Residues: 26-307; Coverage: 87%)
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
Ligand NAG 2 x NAG
Ligand BTB 1 x BTB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P3221
Unit cell:
a: 111.68Å b: 111.68Å c: 54.997Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.177 0.177 0.193
Expression system: Komagataella pastoris

Quick links

Citations

9 review citations

Stabilizing biocatalysts.
Bommarius et al. (2013)
8 more

4 mentions without citation

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