Structure of PDB 2ok9 Chain B

Receptor sequence
>2ok9B (length=121) Species: 113192 (Bothrops pirajai) [Search protein sequence]
SLFELGKMILQETGKNPAKSYGAYGCNCGVLGRGKPKDATDRCCYVHKCC
YKKLTGCNPKKDRYSYSWKDKTIVCGENNPCLKELCECDKAVAICLRENL
GTYNKLYRYHLKPFCKKADDC
3D structure
PDB2ok9 Crystal structure of a phospholipase A(2) homolog complexed with p-bromophenacyl bromide reveals important structural changes associated with the inhibition of myotoxic activity.
ChainB
Resolution2.34 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N28 G30 L32 H48 K49 Y52 Y73 D99
Catalytic site (residue number reindexed from 1) N27 G29 L31 H47 K48 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 PBP B Y22 G23 C29 G30 C45 H48 K49 Y21 G22 C28 G29 C44 H47 K48
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2ok9, PDBe:2ok9, PDBj:2ok9
PDBsum2ok9
PubMed19616648
UniProtP58399|PA2H1_BOTPI Basic phospholipase A2 homolog piratoxin-1

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