PDBe 1g0z

X-ray diffraction
2.18Å resolution

SPECIFIC MUTATIONS IN KRAIT PLA2 LEAD TO DIMERIZATION OF PROTEIN MOLECULES: CRYSTAL STRUCTURE OF KRAIT PLA2 AT 2.1 RESOLUTION

Released:
Source organism: Bungarus caeruleus
Entry authors: Singh TP, Gourinath S, Sharma S, Singh G

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Basic phospholipase A2 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 118 amino acids
Theoretical weight: 12.98 KDa
Source organism: Bungarus caeruleus
UniProt:
  • Canonical: Q6SLM1 (Residues: 20-137; 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: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: R3
Unit cell:
a: 80.36Å b: 80.36Å c: 99.44Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.199 0.257