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2OSH

crystal structure of Natratoxin, a snake sPLA2 that blocks A-type K+ channel

Functional Information from GO Data
ChainGOidnamespacecontents
A0004623molecular_functionphospholipase A2 activity
A0005509molecular_functioncalcium ion binding
A0005543molecular_functionphospholipid binding
A0005576cellular_componentextracellular region
A0006629biological_processlipid metabolic process
A0006644biological_processphospholipid metabolic process
A0015459molecular_functionpotassium channel regulator activity
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
A0035821biological_processmodulation of process of another organism
A0046872molecular_functionmetal ion binding
A0047498molecular_functioncalcium-dependent phospholipase A2 activity
A0050482biological_processarachidonate secretion
A0090729molecular_functiontoxin activity
A0099106molecular_functionion channel regulator activity
Functional Information from PROSITE/UniProt
site_idPS00118
Number of Residues8
DetailsPA2_HIS Phospholipase A2 histidine active site. CCQvHDnC
ChainResidueDetails
ACYS43-CYS50

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. VCDCDRLAaIC
ChainResidueDetails
AVAL89-CYS99

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"2274785","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"2274785","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2274787","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1POA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1POB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
AHIS47
AASP93
AGLY29

243911

PDB entries from 2025-10-29

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