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1DB4

HUMAN S-PLA2 IN COMPLEX WITH INDOLE 8

Functional Information from GO Data
ChainGOidnamespacecontents
A0004623molecular_functionphospholipase A2 activity
A0005509molecular_functioncalcium ion binding
A0005543molecular_functionphospholipid binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005739cellular_componentmitochondrion
A0005741cellular_componentmitochondrial outer membrane
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005886cellular_componentplasma membrane
A0006629biological_processlipid metabolic process
A0006644biological_processphospholipid metabolic process
A0006954biological_processinflammatory response
A0010744biological_processpositive regulation of macrophage derived foam cell differentiation
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
A0030141cellular_componentsecretory granule
A0031640biological_processkilling of cells of another organism
A0034374biological_processlow-density lipoprotein particle remodeling
A0036335biological_processintestinal stem cell homeostasis
A0042130biological_processnegative regulation of T cell proliferation
A0042742biological_processdefense response to bacterium
A0046337biological_processphosphatidylethanolamine metabolic process
A0046470biological_processphosphatidylcholine metabolic process
A0046473biological_processphosphatidic acid metabolic process
A0046872molecular_functionmetal ion binding
A0047498molecular_functioncalcium-dependent phospholipase A2 activity
A0048471cellular_componentperinuclear region of cytoplasm
A0050482biological_processarachidonic acid secretion
A0050729biological_processpositive regulation of inflammatory response
A0050830biological_processdefense response to Gram-positive bacterium
A0070062cellular_componentextracellular exosome
A0070374biological_processpositive regulation of ERK1 and ERK2 cascade
A1902563biological_processregulation of neutrophil activation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 198
ChainResidue
AHIS27
AGLY29
AGLY31
AASP48
A8IN200

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 199
ChainResidue
AHOH229
AHOH260
APHE23
AGLY25
ATYR112
AASN114

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 8IN A 200
ChainResidue
ALEU2
AHIS6
ALEU19
ATYR21
AGLY22
AHIS27
ACYS28
AGLY29
AVAL30
AGLY31
ACYS44
AHIS47
AASP48
ATYR51
ALYS62
ACA198
AHOH212
AHOH219
AHOH246
AHOH259

Functional Information from PROSITE/UniProt
site_idPS00118
Number of Residues8
DetailsPA2_HIS Phospholipase A2 histidine active site. CCVtHDcC
ChainResidueDetails
ACYS43-CYS50

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. LCECDKAAaTC
ChainResidueDetails
ALEU87-CYS97

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AHIS47
AASP91

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:1948070, ECO:0000269|PubMed:7664108, ECO:0000312|PDB:1DB4, ECO:0000312|PDB:1DB5, ECO:0000312|PDB:1DCY, ECO:0000312|PDB:1POE
ChainResidueDetails
AHIS27
AGLY29
AGLY31
AASP48

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Important for integrin binding => ECO:0000269|PubMed:18635536
ChainResidueDetails
AARG74
AARG100

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1n29
ChainResidueDetails
AHIS47
AASP91
AGLY29

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PDB entries from 2024-07-24

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