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3JTI

Crystal structure of the complex formed between Phospholipase A2 with beta-amyloid fragment, Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met at 1.8 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004623molecular_functionphospholipase A2 activity
A0005102molecular_functionsignaling receptor binding
A0005509molecular_functioncalcium ion binding
A0005543molecular_functionphospholipid binding
A0005576cellular_componentextracellular region
A0006633biological_processfatty acid biosynthetic process
A0006644biological_processphospholipid metabolic process
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
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
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 201
ChainResidue
ATYR28
AGLY30
AGLY32
AASP49
AHOH221
BLEU7
BMET8

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. VCDCDRLAaIC
ChainResidueDetails
AVAL90-CYS100

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Implicated in free radical propagation => ECO:0000250
ChainResidueDetails
BGLY6
AASP94

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Susceptible to oxidation => ECO:0000269|PubMed:10535332
ChainResidueDetails
BMET8
AGLY30
AGLY32
AASP49

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PDB entries from 2024-11-06

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