5IXC
Human GIVD cytosolic phospholipase A2 in complex with Methyl gamma-Linolenyl Fluorophosphonate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004620 | molecular_function | phospholipase activity |
A | 0004623 | molecular_function | phospholipase A2 activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005544 | molecular_function | calcium-dependent phospholipid binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0006650 | biological_process | glycerophospholipid metabolic process |
A | 0008970 | molecular_function | phospholipase A1 activity |
A | 0009395 | biological_process | phospholipid catabolic process |
A | 0016020 | cellular_component | membrane |
A | 0016042 | biological_process | lipid catabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0036148 | biological_process | phosphatidylglycerol acyl-chain remodeling |
A | 0036149 | biological_process | phosphatidylinositol acyl-chain remodeling |
A | 0046475 | biological_process | glycerophospholipid catabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0047498 | molecular_function | calcium-dependent phospholipase A2 activity |
A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
B | 0004620 | molecular_function | phospholipase activity |
B | 0004623 | molecular_function | phospholipase A2 activity |
B | 0005509 | molecular_function | calcium ion binding |
B | 0005544 | molecular_function | calcium-dependent phospholipid binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0006650 | biological_process | glycerophospholipid metabolic process |
B | 0008970 | molecular_function | phospholipase A1 activity |
B | 0009395 | biological_process | phospholipid catabolic process |
B | 0016020 | cellular_component | membrane |
B | 0016042 | biological_process | lipid catabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0036148 | biological_process | phosphatidylglycerol acyl-chain remodeling |
B | 0036149 | biological_process | phosphatidylinositol acyl-chain remodeling |
B | 0046475 | biological_process | glycerophospholipid catabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0047498 | molecular_function | calcium-dependent phospholipase A2 activity |
B | 0052689 | molecular_function | carboxylic ester hydrolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue 7FA A 901 |
Chain | Residue |
A | GLY330 |
A | TYR650 |
A | PHE651 |
A | LEU768 |
A | SER769 |
A | GLY331 |
A | SER361 |
A | GLY362 |
A | PHE400 |
A | SER528 |
A | ILE530 |
A | GLY582 |
A | LEU585 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue BA A 902 |
Chain | Residue |
A | ASP165 |
A | HIS167 |
B | ASP165 |
B | HIS167 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue BA A 903 |
Chain | Residue |
A | SER41 |
A | GLU42 |
A | ASP44 |
A | ASP66 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue BA A 904 |
Chain | Residue |
A | ASP96 |
A | THR99 |
A | ASP101 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue BA B 902 |
Chain | Residue |
A | ASP165 |
A | HIS167 |
B | ASP165 |
B | HIS167 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue BA B 903 |
Chain | Residue |
B | SER41 |
B | GLU42 |
B | ASP44 |
B | ASP66 |
B | HOH1032 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue BA B 904 |
Chain | Residue |
B | ASP96 |
B | THR99 |
B | ASP101 |
site_id | AC8 |
Number of Residues | 17 |
Details | binding site for Di-peptide 7FA B 901 and SER B 361 |
Chain | Residue |
B | GLY330 |
B | GLY331 |
B | ILE360 |
B | GLY362 |
B | SER363 |
B | THR364 |
B | TRP365 |
B | TRP527 |
B | SER528 |
B | ILE530 |
B | GLY582 |
B | LEU585 |
B | TYR650 |
B | PHE651 |
B | LEU768 |
B | SER769 |
B | HOH1005 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:27220631, ECO:0007744|PDB:5IXC, ECO:0007744|PDB:5IZR |
Chain | Residue | Details |
A | SER361 | |
B | SER361 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P47712 |
Chain | Residue | Details |
A | ASP647 | |
B | ASP647 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 |
Chain | Residue | Details |
A | ASP38 | |
B | ASP102 | |
A | ASP44 | |
A | ASP94 | |
A | ASP96 | |
A | ASP102 | |
B | ASP38 | |
B | ASP44 | |
B | ASP94 | |
B | ASP96 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27220631, ECO:0007744|PDB:5IXC, ECO:0007744|PDB:5IZR |
Chain | Residue | Details |
A | GLY330 | |
B | GLY330 |