Structure of PDB 2i0u Chain E

Receptor sequence
>2i0uE (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
ChainE
Resolution2.2 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
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 E N10 A16 N10 A15
BS02 TRT E V19 Y22 Y28 G30 C45 V18 Y21 Y27 G29 C44
BS03 TFA E 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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2i0u, PDBe:2i0u, PDBj:2i0u
PDBsum2i0u
PubMed
UniProtQ1RP79|PA2B1_VIPBN Basic phospholipase A2 chain HDP-1P

[Back to BioLiP]