› 1w52

X-ray diffraction
2.99Å resolution

Crystal structure of a proteolyzed form of pancreatic lipase related protein 2 from horse

Released:
DOI: 10.2210/pdb1w52/pdb
PDB entry 1w52 coloured by chain, front view.
PDB entry 1w52 coloured by chain, side view.
PDB entry 1w52 coloured by chain, top view.
Source organism: Equus caballus
Primary publication:
Crystallization of a proteolyzed form of the horse pancreatic lipase-related protein 2: structural basis for the specific detergent requirement.
Mancheño JM, Jayne S, Kerfelec B, Chapus C, Crenon I, Hermoso JA
Acta Crystallogr D Biol Crystallogr 60 2107-9 (2004)
PMID: 15502342

Function and Biology Details

Reactions catalysed: 
1,2-diacyl-3-beta-D-galactosyl-sn-glycerol + 2 H(2)O = 3-beta-D-galactosyl-sn-glycerol + 2 carboxylates
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188253 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pancreatic lipase-related protein 2 Chain: X
Molecule details ›
Chain: X
Length: 452 amino acids
Theoretical weight: 50.11 KDa
Source organism: Equus caballus
UniProt:
  • Canonical: Q95KP4 (Residues: 1-452; Coverage: 100%)
Gene name: PLRP2
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand DDQ 2 x DDQ
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P3221
Unit cell:
a: 128.426Å b: 128.426Å c: 85.818Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.234 0.231 0.294

Quick links

Citations

1 review citation

Structure and Function of Pancreatic Lipase-Related Protein 2 and Its Relationship With Pathological States.
Zhu et al. (2021)
2 other articles