1SKG
Structure-based rational drug design: Crystal structure of the complex formed between Phospholipase A2 and a pentapeptide Val-Ala-Phe-Arg-Ser
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3001 |
| Chain | Residue |
| A | ASP2039 |
| A | ARG2043 |
| A | HOH9069 |
| A | HOH9223 |
| A | HOH9235 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3002 |
| Chain | Residue |
| A | HOH9089 |
| A | HOH9115 |
| A | HOH9146 |
| A | HOH9149 |
| A | HOH9177 |
| A | HOH9223 |
| A | HOH9228 |
| A | GLU2004 |
| A | ARG2072 |
| A | LYS2074 |
| A | HOH9081 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3003 |
| Chain | Residue |
| A | SER2114 |
| A | LYS2115 |
| A | LYS2131 |
| A | HOH9167 |
| A | HOH9256 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3004 |
| Chain | Residue |
| A | ALA2081 |
| A | LYS2086 |
| A | LYS2100 |
| A | ILE2104 |
| A | MOH5678 |
| A | HOH9028 |
| A | HOH9121 |
| A | HOH9126 |
| A | HOH9170 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MOH A 5678 |
| Chain | Residue |
| A | LYS2086 |
| A | GLY2088 |
| A | ASN2093 |
| A | SO43004 |
| A | HOH9028 |
| A | HOH9175 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MOH A 5679 |
| Chain | Residue |
| A | LEU2010 |
| A | LEU2017 |
| A | HOH9100 |
| A | HOH9140 |
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 | GLY2030 | |
| A | HIS2048 | |
| A | ASP2099 |
