Structure of PDB 3jr8 Chain A

Receptor sequence
>3jr8A (length=122) Species: 8726 (Bothrops jararacussu) [Search protein sequence]
DLWQFGQMILKETGKLPFPYYTTYGCYCGWGGQGQPKDATDRCCFVHDCC
YGKLTNCKPKTDRYSYSRENGVIICGEGTPCEKQICECDKAAAVCFRENL
RTYKKRYMAYPDVLCKKPAEKC
3D structure
PDB3jr8 Structural, functional, and bioinformatics studies reveal a new snake venom homologue phospholipase A2 class.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y28 G30 G32 H48 D49 Y52 Y73 D99
Catalytic site (residue number reindexed from 1) Y27 G29 G31 H47 D48 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 CA A Y22 T41 F106 N109 L110 Y113 Y21 T40 F96 N99 L100 Y103
BS02 CA A D39 A40 T41 N109 T112 Y113 D38 A39 T40 N99 T102 Y103
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
GO:0090729 toxin activity
Biological Process
GO:0006644 phospholipid metabolic process
GO:0016042 lipid catabolic process
GO:0035821 modulation of process of another organism
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:3jr8, PDBe:3jr8, PDBj:3jr8
PDBsum3jr8
PubMed20878713
UniProtP45881|PA2B2_BOTJR Basic phospholipase A2 homolog bothropstoxin-II

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