5IZ5
Human GIVD cytosolic phospholipase A2
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 |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 901 |
| Chain | Residue |
| B | PRO662 |
| B | GLY663 |
| B | ARG665 |
| B | HOH1171 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 B 902 |
| Chain | Residue |
| B | ARG449 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 903 |
| Chain | Residue |
| B | HOH1216 |
| B | GLN600 |
| B | PRO641 |
| B | ARG642 |
| B | HOH1168 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 904 |
| Chain | Residue |
| B | ASN470 |
| B | PHE621 |
| B | PRO633 |
| B | SER634 |
| B | GLN635 |
| B | HOH1014 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 905 |
| Chain | Residue |
| A | ARG596 |
| B | THR474 |
| B | LEU475 |
| B | ASP476 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 906 |
| Chain | Residue |
| B | ARG245 |
| B | THR248 |
| B | LYS251 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 907 |
| Chain | Residue |
| B | ARG415 |
| B | PRO518 |
| B | ARG519 |
| B | PHE522 |
| B | HOH1118 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 908 |
| Chain | Residue |
| B | HIS281 |
| B | ASN285 |
| B | HOH1008 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 909 |
| Chain | Residue |
| B | ILE526 |
| B | ARG601 |
| B | SER602 |
| B | LEU643 |
| B | CYS644 |
| B | LEU645 |
| B | HOH1004 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 B 910 |
| Chain | Residue |
| B | MET335 |
| B | TYR339 |
| B | TRP365 |
| B | THR366 |
| B | HIS369 |
| B | ALA388 |
| B | HOH1012 |
| B | HOH1153 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 901 |
| Chain | Residue |
| A | GLN129 |
| A | SER395 |
| A | LYS396 |
| A | LEU397 |
| A | SER577 |
| A | THR772 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 902 |
| Chain | Residue |
| A | PRO662 |
| A | GLY663 |
| A | ARG665 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 903 |
| Chain | Residue |
| A | GLN50 |
| A | PRO55 |
| A | GLY56 |
| A | MET57 |
| A | LYS58 |
| site_id | AD5 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 A 904 |
| Chain | Residue |
| A | PHE737 |
| A | LYS738 |
| A | HIS740 |
| A | SER741 |
| A | ARG747 |
| A | GLU751 |
| A | LEU752 |
| A | GLY754 |
| A | GLY755 |
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 |
| B | SER361 | |
| A | SER361 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P47712 |
| Chain | Residue | Details |
| B | ASP647 | |
| A | ASP647 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 |
| Chain | Residue | Details |
| B | ASP38 | |
| A | ASP102 | |
| B | ASP44 | |
| B | ASP94 | |
| B | ASP96 | |
| B | ASP102 | |
| A | ASP38 | |
| A | ASP44 | |
| A | ASP94 | |
| A | 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 |
| B | GLY330 | |
| A | GLY330 |
