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1VKQ

A re-determination of the structure of the triple mutant (K53,56,120M) of phospholipase A2 at 1.6A resolution using sulphur-SAS at 1.54A wavelength

Functional Information from GO Data
ChainGOidnamespacecontents
A0002227biological_processinnate immune response in mucosa
A0004623molecular_functionphospholipase A2 activity
A0005102molecular_functionsignaling receptor binding
A0005509molecular_functioncalcium ion binding
A0005543molecular_functionphospholipid binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006629biological_processlipid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0006644biological_processphospholipid metabolic process
A0008284biological_processpositive regulation of cell population proliferation
A0009986cellular_componentcell surface
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
A0019731biological_processantibacterial humoral response
A0032052molecular_functionbile acid binding
A0046470biological_processphosphatidylcholine metabolic process
A0046471biological_processphosphatidylglycerol metabolic process
A0046872molecular_functionmetal ion binding
A0047498molecular_functioncalcium-dependent phospholipase A2 activity
A0048146biological_processpositive regulation of fibroblast proliferation
A0050482biological_processarachidonate secretion
A0050830biological_processdefense response to Gram-positive bacterium
A0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
A1904635biological_processpositive regulation of podocyte apoptotic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 224
ChainResidue
ATYR28
AGLY30
AGLY32
AASP49
AHOH245
AHOH248

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 225
ChainResidue
AHOH332
ALYS12
AILE82
AILE104

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD A 226
ChainResidue
APHE5
APHE22
AGLY30
AHOH245

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MPD A 227
ChainResidue
ALEU19
ALYS108

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 228
ChainResidue
ASER15
AASP21
AGLN54
APHE94
AHOH265

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

site_idPS00119
Number of Residues11
DetailsPA2_ASP Phospholipase A2 aspartic acid active site. ICNCDRNAaIC
ChainResidueDetails
AILE95-CYS105

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"7464926","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10089353","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7265241","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9115986","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BP2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KVW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MKS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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

238895

PDB entries from 2025-07-16

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