› 1g2x

X-ray diffraction
2.5Å resolution

Sequence induced trimerization of krait PLA2: crystal structure of the trimeric form of krait PLA2

Released:
DOI: 10.2210/pdb1g2x/pdb
PDB entry 1g2x coloured by chain, front view.
PDB entry 1g2x coloured by chain, side view.
PDB entry 1g2x coloured by chain, top view.
Source organism: Bungarus caeruleus
Primary publication:
Sequence-induced trimerization of phospholipase A2: structure of a trimeric isoform of PLA2 from common krait (Bungarus caeruleus) at 2.5 A resolution.
Singh G, Gourinath S, Saravanan K, Sharma S, Bhanumathi S, Betzel Ch, Srinivasan A, Singh TP
Acta Crystallogr Sect F Struct Biol Cryst Commun 61 8-13 (2005)
PMID: 16508078

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180330 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Basic phospholipase A2 3 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 118 amino acids
Theoretical weight: 12.98 KDa
Source organism: Bungarus caeruleus
UniProt:
  • Canonical: Q6SLM0 (Residues: 20-137; Coverage: 94%)
Sequence domains: Phospholipase A2
Structure domains: Phospholipase A2 domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: C2
Unit cell:
a: 80.949Å b: 80.572Å c: 57.098Å
α: 90° β: 90.35° γ: 90°
R-values:
R R work R free
0.201 0.198 0.262

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Citations

4 citation in other articles

Comparison of proteomic profiles of the venoms of two of the 'Big Four' snakes of India, the Indian cobra (Naja naja) and the common krait (Bungarus caeruleus), and analyses of their toxins.
Choudhury et al. (2017)
3 more

7 mentions without citation

The interface of protein structure, protein biophysics, and molecular evolution.
Liberles et al. (2012)
6 more