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1PO8

Crystal structure of a complex formed between krait venom phospholipase A2 and heptanoic acid at 2.7 A resolution.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004623molecular_functionphospholipase A2 activity
A0005509molecular_functioncalcium ion binding
A0005543molecular_functionphospholipid binding
A0005576cellular_componentextracellular region
A0006644biological_processphospholipid metabolic process
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_processarachidonic acid secretion
A0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 121
ChainResidue
ATYR28
AGLY30
AGLY32
AGLY33
AASP49

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SHV A 122
ChainResidue
AARG43
ACYS45
AHIS48
ACYS29
AGLY30
ALYS31
AASP40

Functional Information from PROSITE/UniProt
site_idPS00118
Number of Residues8
DetailsPA2_HIS Phospholipase A2 histidine active site. CCYtHDhC
ChainResidueDetails
ACYS44-CYS51

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. VCDCDRTAaIC
ChainResidueDetails
AVAL90-CYS100

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:11286555
ChainResidueDetails
ALYS56
AALA102

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11286555, ECO:0007744|PDB:1FE5
ChainResidueDetails
ATHR36
AVAL38
AASP40
AASN57

221051

PDB entries from 2024-06-12

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