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1B4W

BASIC PHOSPHOLIPASE A2 FROM AGKISTRODON HALYS PALLAS-IMPLICATIONS FOR ITS ASSOCIATION AND ANTICOAGULANT ACTIVITIES BY X-RAY CRYSTALLOGRAPHY

Functional Information from GO Data
ChainGOidnamespacecontents
A0004623molecular_functionphospholipase A2 activity
A0005102molecular_functionsignaling receptor binding
A0005509molecular_functioncalcium ion binding
A0005543molecular_functionphospholipid binding
A0005576cellular_componentextracellular region
A0006633biological_processfatty acid biosynthetic process
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
A0048146biological_processpositive regulation of fibroblast proliferation
A0050482biological_processarachidonic acid secretion
A0090729molecular_functiontoxin activity
B0004623molecular_functionphospholipase A2 activity
B0005102molecular_functionsignaling receptor binding
B0005509molecular_functioncalcium ion binding
B0005543molecular_functionphospholipid binding
B0005576cellular_componentextracellular region
B0006633biological_processfatty acid biosynthetic process
B0006644biological_processphospholipid metabolic process
B0016042biological_processlipid catabolic process
B0016787molecular_functionhydrolase activity
B0035821biological_processmodulation of process of another organism
B0046872molecular_functionmetal ion binding
B0047498molecular_functioncalcium-dependent phospholipase A2 activity
B0048146biological_processpositive regulation of fibroblast proliferation
B0050482biological_processarachidonic acid secretion
B0090729molecular_functiontoxin activity
C0004623molecular_functionphospholipase A2 activity
C0005102molecular_functionsignaling receptor binding
C0005509molecular_functioncalcium ion binding
C0005543molecular_functionphospholipid binding
C0005576cellular_componentextracellular region
C0006633biological_processfatty acid biosynthetic process
C0006644biological_processphospholipid metabolic process
C0016042biological_processlipid catabolic process
C0016787molecular_functionhydrolase activity
C0035821biological_processmodulation of process of another organism
C0046872molecular_functionmetal ion binding
C0047498molecular_functioncalcium-dependent phospholipase A2 activity
C0048146biological_processpositive regulation of fibroblast proliferation
C0050482biological_processarachidonic acid secretion
C0090729molecular_functiontoxin activity
D0004623molecular_functionphospholipase A2 activity
D0005102molecular_functionsignaling receptor binding
D0005509molecular_functioncalcium ion binding
D0005543molecular_functionphospholipid binding
D0005576cellular_componentextracellular region
D0006633biological_processfatty acid biosynthetic process
D0006644biological_processphospholipid metabolic process
D0016042biological_processlipid catabolic process
D0016787molecular_functionhydrolase activity
D0035821biological_processmodulation of process of another organism
D0046872molecular_functionmetal ion binding
D0047498molecular_functioncalcium-dependent phospholipase A2 activity
D0048146biological_processpositive regulation of fibroblast proliferation
D0050482biological_processarachidonic acid secretion
D0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsACTIVE SITE 1
ChainResidue
AHIS48
AASP99

site_idAC2
Number of Residues2
DetailsACTIVE SITE 2
ChainResidue
BHIS48
BASP99

site_idAC3
Number of Residues2
DetailsACTIVE SITE 3
ChainResidue
CHIS48
CASP99

site_idAC4
Number of Residues2
DetailsACTIVE SITE 4
ChainResidue
DHIS48
DASP99

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

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. VCECDKAAaIC
ChainResidueDetails
AVAL95-CYS105

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P06859
ChainResidueDetails
AASP72
ALYS115
BASP72
BLYS115
CASP72
CLYS115
DASP72
DLYS115

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:9761847, ECO:0007744|PDB:1JIA
ChainResidueDetails
DCYS44
DPHE46
DHIS48
DTYR73
ACYS44
APHE46
AHIS48
ATYR73
BCYS44
BPHE46
BHIS48
BTYR73
CCYS44
CPHE46
CHIS48
CTYR73

220472

PDB entries from 2024-05-29

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