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1CEH

STRUCTURE AND FUNCTION OF THE CATALYTIC SITE MUTANT ASP99ASN OF PHOSPHOLIPASE A2: ABSENCE OF CONSERVED STRUCTURAL WATER

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
A0047499molecular_functioncalcium-independent 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 124
ChainResidue
ATYR28
AGLY30
AGLY32
AASP49
AHOH204
AHOH238

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:7464926
ChainResidueDetails
AHIS48
AASN99

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10089353, ECO:0000269|PubMed:7265241, ECO:0000269|PubMed:9115986, ECO:0007744|PDB:1BP2, ECO:0007744|PDB:1KVW, ECO:0007744|PDB:1MKS
ChainResidueDetails
ATYR28
AGLY30
AGLY32
AASP49

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bp2
ChainResidueDetails
AHIS48
AGLY30
AASN99

227111

PDB entries from 2024-11-06

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