Structure of PDB 3bjw Chain E

Receptor sequence
>3bjwE (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
ChainE
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 E V3 Q11 V3 Q11
BS02 SVR E V2 L5 G6 I10 K16 S17 P18 F19 P20 S21 T23 K115 V2 L5 G6 I10 K15 S16 P17 F18 P19 S20 T22 K105
BS03 SVR E K7 I10 Q11 E12 T13 G14 R107 L110 K7 I10 Q11 E12 T13 G14 R97 L100
BS04 SVR E P121 N122 F124 P111 N112 F113
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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