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1N28

Crystal structure of the H48Q mutant of human group IIA phospholipase A2

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
B0004623molecular_functionphospholipase A2 activity
B0005509molecular_functioncalcium ion binding
B0005543molecular_functionphospholipid binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005739cellular_componentmitochondrion
B0005741cellular_componentmitochondrial outer membrane
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005886cellular_componentplasma membrane
B0006629biological_processlipid metabolic process
B0006644biological_processphospholipid metabolic process
B0006954biological_processinflammatory response
B0010744biological_processpositive regulation of macrophage derived foam cell differentiation
B0016042biological_processlipid catabolic process
B0016787molecular_functionhydrolase activity
B0030141cellular_componentsecretory granule
B0031640biological_processkilling of cells of another organism
B0034374biological_processlow-density lipoprotein particle remodeling
B0036335biological_processintestinal stem cell homeostasis
B0042130biological_processnegative regulation of T cell proliferation
B0042742biological_processdefense response to bacterium
B0046337biological_processphosphatidylethanolamine metabolic process
B0046470biological_processphosphatidylcholine metabolic process
B0046473biological_processphosphatidic acid metabolic process
B0046872molecular_functionmetal ion binding
B0047498molecular_functioncalcium-dependent phospholipase A2 activity
B0048471cellular_componentperinuclear region of cytoplasm
B0050482biological_processarachidonic acid secretion
B0050729biological_processpositive regulation of inflammatory response
B0050830biological_processdefense response to Gram-positive bacterium
B0070062cellular_componentextracellular exosome
B0070374biological_processpositive regulation of ERK1 and ERK2 cascade
B1902563biological_processregulation of neutrophil activation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 125
ChainResidue
BHIS27
BGLY29
BGLY31
BASP48
BHOH161

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 126
ChainResidue
AHOH140
AHIS27
AGLY29
AGLY31
AASP48

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 127
ChainResidue
BPHE23
BGLY25
BTYR112
BASN114
BHOH171

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 128
ChainResidue
APHE23
AGLY25
ATYR112
AASN114
AHOH165
AHOH166

Functional Information from PROSITE/UniProt
site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. LCECDKAAaTC
ChainResidueDetails
BLEU87-CYS97

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
BGLN47
BASP91
AGLN47
AASP91

site_idSWS_FT_FI2
Number of Residues8
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
BHIS27
BGLY29
BGLY31
AGLY31
AASP48
BASP48
AHIS27
AGLY29

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Important for integrin binding => ECO:0000269|PubMed:18635536
ChainResidueDetails
AARG74
AARG100
BARG74
BARG100

219869

PDB entries from 2024-05-15

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