1Y75
A new form of catalytically inactive phospholipase A2 with an unusual disulphide bridge Cys 32- Cys 49 reveals recognition for N-acetylglucosmine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004623 | molecular_function | phospholipase A2 activity |
| A | 0005102 | molecular_function | signaling receptor binding |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005543 | molecular_function | phospholipid binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0006644 | biological_process | phospholipid metabolic process |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047498 | molecular_function | calcium-dependent phospholipase A2 activity |
| A | 0048146 | biological_process | positive regulation of fibroblast proliferation |
| A | 0050482 | biological_process | arachidonate secretion |
| B | 0004623 | molecular_function | phospholipase A2 activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005543 | molecular_function | phospholipid binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006644 | biological_process | phospholipid metabolic process |
| B | 0016042 | biological_process | lipid catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047498 | molecular_function | calcium-dependent phospholipase A2 activity |
| B | 0050482 | biological_process | arachidonate secretion |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"Q6T179","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16287060","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Y75","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q6T179","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1n29 |
| Chain | Residue | Details |
| B | HIS48 | |
| B | GLY30 | |
| B | ASP94 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1n29 |
| Chain | Residue | Details |
| A | HIS48 | |
| A | GLY30 | |
| A | ASP94 |
