1JQ9
Crystal structure of a complex formed between phospholipase A2 from Daboia russelli pulchella and a designed pentapeptide Phe-Leu-Ser-Tyr-Lys at 1.8 resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004623 | molecular_function | A2-type glycerophospholipase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005543 | molecular_function | phospholipid binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006644 | biological_process | phospholipid metabolic process |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0042130 | biological_process | negative regulation of T cell proliferation |
| A | 0050482 | biological_process | arachidonate secretion |
| B | 0004623 | molecular_function | A2-type glycerophospholipase activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005543 | molecular_function | phospholipid binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006644 | biological_process | phospholipid metabolic process |
| B | 0016042 | biological_process | lipid catabolic process |
| B | 0042130 | biological_process | negative regulation of T cell proliferation |
| B | 0050482 | biological_process | arachidonate secretion |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACY A 301 |
| Chain | Residue |
| A | LYS116 |
| A | HOH425 |
| B | GLU11 |
| B | HOH379 |
| B | HOH382 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACY A 302 |
| Chain | Residue |
| B | HOH369 |
| B | HOH389 |
| A | PRO121 |
| A | PHE124 |
| A | HOH365 |
| B | ARG107 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACY B 303 |
| Chain | Residue |
| B | SER90 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACY A 304 |
| Chain | Residue |
| A | ARG43 |
| A | HOH330 |
| A | HOH361 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR CHAIN P OF PEPTIDE INHIBITOR |
| Chain | Residue |
| A | LEU2 |
| A | LEU3 |
| A | PHE5 |
| A | GLY6 |
| A | LYS7 |
| A | ILE9 |
| A | ALA18 |
| A | ILE19 |
| A | TYR28 |
| A | CYS29 |
| A | GLY30 |
| A | TRP31 |
| A | GLY32 |
| A | HIS48 |
| A | ASP49 |
| A | LYS69 |
| B | ARG43 |
| B | PHE46 |
| B | VAL47 |
| B | ASN54 |
| B | CYS133 |
| B | HOH306 |
| P | HOH64 |
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":"P14418","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| 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 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1n29 |
| Chain | Residue | Details |
| B | HIS48 | |
| B | GLY30 | |
| B | ASP99 |
