Structure of PDB 2i0u Chain A

Receptor sequence
>2i0uA (length=122) [Search protein sequence]
NLFQFAKMINGKLGAFSVWNYISYGCYCGWGGQGTPKDATDRCCFVHDCC
YGRVRGCNPKLAIYAYSFKKGNIVCGKNNGCLRDICECDRVAANCFHQNQ
NTYNKNYKFLSSSRCRQTSEQC
3D structure
PDB2i0u Crystal structures of phospholipases A2 from Vipera nikolskii venom revealing Triton X-100 bound in hydrophobic channel
ChainA
Resolution2.2 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 N10 A16 N10 A15
BS02 TRT A L2 Y22 I23 Y28 G30 G32 C45 D49 L2 Y21 I22 Y27 G29 G31 C44 D48
BS03 TFA A F17 W20 F16 W19
Gene Ontology
Molecular Function
GO:0004623 phospholipase A2 activity
GO:0005509 calcium ion binding
GO:0005543 phospholipid binding
GO:0016787 hydrolase activity
GO:0046872 metal ion 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:0050482 arachidonate secretion
Cellular Component
GO:0005576 extracellular region

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Cellular Component
External links
PDB RCSB:2i0u, PDBe:2i0u, PDBj:2i0u
PDBsum2i0u
PubMed
UniProtQ1RP79|PA2B1_VIPBN Basic phospholipase A2 chain HDP-1P

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