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PDBe Entry: 1fb2 view

STRUCTURE OF PHOSPHOLIPASE A2 FROM DABOIA RUSSELLI PULCHELLA AT 1.95
Summary
Header TOXINsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.95 Å, R-factor: 23.4%, Free R-factor: 27.2%, Spacegroup: C 2 2 21
Released 25/07/2001, deposition: 14/07/2000, last revision: 24/02/2009
Authors Chandra, V.search; Kaur, Psearch; Betzel, C.search; Singh, T.P.search
Primary citation Regulation of catalytic function by molecular association: structure of phospholipase A2 from Daboia russelli pulchella (DPLA2) at 1.9 A resolution.
ACTA CRYSTALLOGR.,SECT.Dsearch vol:57, pag:1793-1798 (2001) [PubMed ID 11717491 ]search
Keywords Structuresearch, Phospholipase A2search, Daboia Russelli Pulchellasearch, Neurotoxicsearch, TOXINsearch
EC 3.1.1.4 ExPASy BRENDA search (A B)
Organism Daboia russellii pulchella 97228search(A B)
UniProt Phospholipase A2 VRV-PL-VIIIa (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (DPLA2) (P1) P59071search (A B)
Solvent A, B
Related entries 1cl5
Polymers
Id Name Type UniProt Residues Observed
A, B PHOSPHOLIPASE A2 Protein P59071 (PA28_DABRR)search
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