Structure of PDB 3bjw Chain C

Receptor sequence
>3bjwC (length=122) Species: 40353 (Echis carinatus) [Search protein sequence]
SVVELGKMIIQETGKSPFPSYTSYGCFCGGGERGPPLDATDRCCLAHSCC
YDTLPDCSPKTDRYKYKRENGEIICENSTSCKKRICECDKAVAVCLRKNL
NTYNKKYTYYPNFWCKGDIEKC
3D structure
PDB3bjw Structural Characterization of Myotoxic Ecarpholin S from Echis carinatus Venom
ChainC
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F28 G30 G32 H48 S49 Y52 Y73 D99
Catalytic site (residue number reindexed from 1) F27 G29 G31 H47 S48 Y51 Y64 D89
Enzyme Commision number 3.1.1.4: phospholipase A2.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 SVR C F124 W125 K127 F113 W114 K116
BS02 SVR C V2 V3 G6 K69 R72 V2 V3 G6 K60 R63
BS03 SVR C S17 F19 P20 S16 F18 P19
BS04 SVR C V2 T70 V2 T61
BS05 SVR C Y113 N114 K115 P121 W125 Y103 N104 K105 P111 W114
Gene Ontology
Molecular Function
GO:0004623 phospholipase A2 activity
GO:0005509 calcium ion binding
GO:0005543 phospholipid binding
GO:0047498 calcium-dependent phospholipase A2 activity
Biological Process
GO:0006644 phospholipid metabolic process
GO:0016042 lipid catabolic process
GO:0042130 negative regulation of T cell proliferation
GO:0050482 arachidonate secretion
Cellular Component
GO:0005576 extracellular region

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Cellular Component
External links
PDB RCSB:3bjw, PDBe:3bjw, PDBj:3bjw
PDBsum3bjw
PubMed18586854
UniProtP48650|PA2HS_ECHCA Basic phospholipase A2 homolog ecarpholin S

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