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PDBe Entry: 1dpy view

THREE-DIMENSIONAL STRUCTURE OF A NOVEL PHOSPHOLIPASE A2 FROM INDIAN COMMON KRAIT AT 2.45 A RESOLUTION
Summary
Header HYDROLASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.45 Å, R-factor: 20.9%, Free R-factor: 28.1%, Spacegroup: R 3 2
Released 28/06/2000, deposition: 28/12/1999, last revision: 24/02/2009
Authors Singh, G.search; Gourinath, S.search; Sharma, S.search; Paramasivam, M.search; Srinivasan, A.search; Singh, T.P.search
Primary citation Sequence and crystal structure determination of a basic phospholipase A2 from common krait (Bungarus caeruleus) at 2.4 A resolution: identification and characterization of its pharmacological sites.
J.MOL.BIOL.search vol:307, pag:1049-1059 (2001) [PubMed ID 11286555 ]search
Keywords INDIAN COMMON KRAIT VENOMsearch, PHOSPHOLIPASE A2search, CRYSTAL STRUCTUREsearch, REFINEMENTsearch, HYDROLASEsearch
EC 3.1.1.4 ExPASy BRENDA search (A)
Organism Bungarus caeruleus 132961search(A)
UniProt Phospholipase A2 KPA2 precursor (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) Q9DF52search (A)
Solvent A
Polymers
Id Name Type UniProt Residues Observed
A PHOSPHOLIPASE A2 Protein Q9DF52 (PA2K_BUNCE)search
118 99%
Heterogens
Id Name Ligands
A SODIUM ION NA search
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