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1RGB

Phospholipase A2 from Vipera ammodytes meridionalis

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
A0031640biological_processkilling of cells of another organism
A0035821biological_processmodulation of process of another organism
A0042130biological_processnegative regulation of T cell proliferation
A0046872molecular_functionmetal ion binding
A0047498molecular_functioncalcium-dependent phospholipase A2 activity
A0047499molecular_functioncalcium-independent phospholipase A2 activity
A0050482biological_processarachidonate secretion
A0090729molecular_functiontoxin activity
B0004623molecular_functionphospholipase A2 activity
B0005509molecular_functioncalcium ion binding
B0005543molecular_functionphospholipid binding
B0005576cellular_componentextracellular region
B0006644biological_processphospholipid metabolic process
B0016042biological_processlipid catabolic process
B0016787molecular_functionhydrolase activity
B0031640biological_processkilling of cells of another organism
B0035821biological_processmodulation of process of another organism
B0042130biological_processnegative regulation of T cell proliferation
B0046872molecular_functionmetal ion binding
B0047498molecular_functioncalcium-dependent phospholipase A2 activity
B0047499molecular_functioncalcium-independent phospholipase A2 activity
B0050482biological_processarachidonate secretion
B0090729molecular_functiontoxin activity
K0004623molecular_functionphospholipase A2 activity
K0005509molecular_functioncalcium ion binding
K0005543molecular_functionphospholipid binding
K0005576cellular_componentextracellular region
K0006644biological_processphospholipid metabolic process
K0016042biological_processlipid catabolic process
K0016787molecular_functionhydrolase activity
K0031640biological_processkilling of cells of another organism
K0035821biological_processmodulation of process of another organism
K0042130biological_processnegative regulation of T cell proliferation
K0046872molecular_functionmetal ion binding
K0047498molecular_functioncalcium-dependent phospholipase A2 activity
K0047499molecular_functioncalcium-independent phospholipase A2 activity
K0050482biological_processarachidonate secretion
K0090729molecular_functiontoxin activity
L0004623molecular_functionphospholipase A2 activity
L0005509molecular_functioncalcium ion binding
L0005543molecular_functionphospholipid binding
L0005576cellular_componentextracellular region
L0006644biological_processphospholipid metabolic process
L0016042biological_processlipid catabolic process
L0016787molecular_functionhydrolase activity
L0031640biological_processkilling of cells of another organism
L0035821biological_processmodulation of process of another organism
L0042130biological_processnegative regulation of T cell proliferation
L0046872molecular_functionmetal ion binding
L0047498molecular_functioncalcium-dependent phospholipase A2 activity
L0047499molecular_functioncalcium-independent phospholipase A2 activity
L0050482biological_processarachidonate secretion
L0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ELD B 134
ChainResidue
AGLY30
BCYS45
BHIS48
BASP49
BLYS69
BALA102
BPHE106
ATRP31
ACYS45
AHIS48
AASP49
BLEU2
BPHE5
BTRP31
BCYS44

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ELD L 134
ChainResidue
KLEU2
KTYR28
KCYS29
KGLY30
KTRP31
KCYS45
KHIS48
KLYS69
LLEU2
LPHE5
LTYR22
LGLY30
LTRP31
LCYS44
LCYS45
LALA102
LPHE106

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. ICECDRVAaNC
ChainResidueDetails
AILE95-CYS105

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:9276469
ChainResidueDetails
AHIS48
AASP99
BHIS48
BASP99
KHIS48
KASP99
LHIS48
LASP99

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P14418
ChainResidueDetails
ATYR28
KGLY30
KGLY32
KASP49
LTYR28
LGLY30
LGLY32
LASP49
AGLY30
AGLY32
AASP49
BTYR28
BGLY30
BGLY32
BASP49
KTYR28

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
AHIS48
AGLY30
AASP99

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
BHIS48
BGLY30
BASP99

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
KHIS48
KGLY30
KASP99

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
LHIS48
LGLY30
LASP99

227344

PDB entries from 2024-11-13

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