Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5IXC

Human GIVD cytosolic phospholipase A2 in complex with Methyl gamma-Linolenyl Fluorophosphonate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004620molecular_functionphospholipase activity
A0004623molecular_functionphospholipase A2 activity
A0005509molecular_functioncalcium ion binding
A0005544molecular_functioncalcium-dependent phospholipid binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006631biological_processfatty acid metabolic process
A0006650biological_processglycerophospholipid metabolic process
A0008970molecular_functionphospholipase A1 activity
A0009395biological_processphospholipid catabolic process
A0016020cellular_componentmembrane
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
A0036148biological_processphosphatidylglycerol acyl-chain remodeling
A0036149biological_processphosphatidylinositol acyl-chain remodeling
A0046475biological_processglycerophospholipid catabolic process
A0046872molecular_functionmetal ion binding
A0047498molecular_functioncalcium-dependent phospholipase A2 activity
A0052689molecular_functioncarboxylic ester hydrolase activity
B0004620molecular_functionphospholipase activity
B0004623molecular_functionphospholipase A2 activity
B0005509molecular_functioncalcium ion binding
B0005544molecular_functioncalcium-dependent phospholipid binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006631biological_processfatty acid metabolic process
B0006650biological_processglycerophospholipid metabolic process
B0008970molecular_functionphospholipase A1 activity
B0009395biological_processphospholipid catabolic process
B0016020cellular_componentmembrane
B0016042biological_processlipid catabolic process
B0016787molecular_functionhydrolase activity
B0036148biological_processphosphatidylglycerol acyl-chain remodeling
B0036149biological_processphosphatidylinositol acyl-chain remodeling
B0046475biological_processglycerophospholipid catabolic process
B0046872molecular_functionmetal ion binding
B0047498molecular_functioncalcium-dependent phospholipase A2 activity
B0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue 7FA A 901
ChainResidue
AGLY330
ATYR650
APHE651
ALEU768
ASER769
AGLY331
ASER361
AGLY362
APHE400
ASER528
AILE530
AGLY582
ALEU585

site_idAC2
Number of Residues4
Detailsbinding site for residue BA A 902
ChainResidue
AASP165
AHIS167
BASP165
BHIS167

site_idAC3
Number of Residues4
Detailsbinding site for residue BA A 903
ChainResidue
ASER41
AGLU42
AASP44
AASP66

site_idAC4
Number of Residues3
Detailsbinding site for residue BA A 904
ChainResidue
AASP96
ATHR99
AASP101

site_idAC5
Number of Residues4
Detailsbinding site for residue BA B 902
ChainResidue
AASP165
AHIS167
BASP165
BHIS167

site_idAC6
Number of Residues5
Detailsbinding site for residue BA B 903
ChainResidue
BSER41
BGLU42
BASP44
BASP66
BHOH1032

site_idAC7
Number of Residues3
Detailsbinding site for residue BA B 904
ChainResidue
BASP96
BTHR99
BASP101

site_idAC8
Number of Residues17
Detailsbinding site for Di-peptide 7FA B 901 and SER B 361
ChainResidue
BGLY330
BGLY331
BILE360
BGLY362
BSER363
BTHR364
BTRP365
BTRP527
BSER528
BILE530
BGLY582
BLEU585
BTYR650
BPHE651
BLEU768
BSER769
BHOH1005

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:27220631, ECO:0007744|PDB:5IXC, ECO:0007744|PDB:5IZR
ChainResidueDetails
ASER361
BSER361

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P47712
ChainResidueDetails
AASP647
BASP647

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00041
ChainResidueDetails
AASP38
BASP102
AASP44
AASP94
AASP96
AASP102
BASP38
BASP44
BASP94
BASP96

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:27220631, ECO:0007744|PDB:5IXC, ECO:0007744|PDB:5IZR
ChainResidueDetails
AGLY330
BGLY330

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon