1SV3
Structure of the complex formed between Phospholipase A2 and 4-methoxybenzoic acid at 1.3A resolution.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004623 | molecular_function | phospholipase A2 activity |
| 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 | 0006644 | biological_process | phospholipid metabolic process |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0035821 | biological_process | modulation of process of another organism |
| A | 0042130 | biological_process | negative regulation of T cell proliferation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047498 | molecular_function | calcium-dependent phospholipase A2 activity |
| A | 0050482 | biological_process | arachidonate secretion |
| A | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 342 |
| Chain | Residue |
| A | GLU4 |
| A | ARG72 |
| A | LYS74 |
| A | HOH361 |
| A | HOH363 |
| A | HOH405 |
| A | HOH441 |
| A | HOH494 |
| A | HOH525 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 343 |
| Chain | Residue |
| A | ARG43 |
| A | HOH422 |
| A | HOH467 |
| A | HOH522 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 344 |
| Chain | Residue |
| A | TYR113 |
| A | SER114 |
| A | LYS115 |
| A | LYS131 |
| A | HOH526 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 345 |
| Chain | Residue |
| A | ALA81 |
| A | LYS86 |
| A | LYS100 |
| A | SO4346 |
| A | HOH357 |
| A | HOH456 |
| A | HOH475 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 346 |
| Chain | Residue |
| A | LYS86 |
| A | SER90 |
| A | ASN93 |
| A | SO4345 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ANN A 347 |
| Chain | Residue |
| A | LEU2 |
| A | TYR22 |
| A | GLY30 |
| A | PHE106 |
| A | HOH511 |
| A | HOH548 |
| A | HOH554 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P14418","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2004","submissionDatabase":"PDB data bank","title":"Crystal structure of a complex formed between group II phospholipase A2 and aspirin at 1.86 A resolution.","authors":["Singh N.","Jabeen T.","Sharma S.","Bhushan A.","Singh T.P."]}},{"source":"PDB","id":"1TGM","evidenceCode":"ECO:0007744"}]} |
| 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 |
| A | HIS48 | |
| A | GLY30 | |
| A | ASP99 |
