1dpy

X-ray diffraction
2.45Å resolution

THREE-DIMENSIONAL STRUCTURE OF A NOVEL PHOSPHOLIPASE A2 FROM INDIAN COMMON KRAIT AT 2.45 A RESOLUTION

Released:

Function and Biology Details

Reaction catalysed:
Phosphatidylcholine + H(2)O = 1-acylglycerophosphocholine + a carboxylate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Basic phospholipase A2 KPA2 Chain: A
Molecule details ›
Chain: A
Length: 118 amino acids
Theoretical weight: 12.95 KDa
Source organism: Bungarus caeruleus
UniProt:
  • Canonical: Q9DF52 (Residues: 28-145; Coverage: 94%)
Sequence domains: Phospholipase A2
Structure domains: Phospholipase A2 domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Unit cell:
a: 57.98Å b: 57.98Å c: 57.98Å
α: 92.02° β: 92.02° γ: 92.02°
R-values:
R R work R free
0.209 0.202 0.281