1TG1
Crystal Structure of the complex formed between russells viper phospholipase A2 and a designed peptide inhibitor PHQ-Leu-Val-Arg-Tyr at 1.2A 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 301 |
| Chain | Residue |
| A | ARG43 |
| A | HOH401 |
| A | HOH414 |
| C | PHQ1 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 302 |
| Chain | Residue |
| A | HOH389 |
| A | HOH418 |
| A | GLU4 |
| A | ARG72 |
| A | LYS74 |
| A | HOH374 |
| A | HOH383 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 303 |
| Chain | Residue |
| A | SER114 |
| A | LYS115 |
| A | LYS131 |
| A | HOH497 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACY A 304 |
| Chain | Residue |
| A | LYS38 |
| A | TYR117 |
| A | HOH410 |
| site_id | AC5 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR CHAIN C OF PEPTIDE INHIBITOR |
| Chain | Residue |
| A | LEU2 |
| A | LEU3 |
| A | ILE19 |
| A | TYR22 |
| A | SER23 |
| A | TYR28 |
| A | CYS29 |
| A | GLY30 |
| A | TRP31 |
| A | GLY32 |
| A | CYS45 |
| A | HIS48 |
| A | ASP49 |
| A | TYR52 |
| A | ASN111 |
| A | THR112 |
| A | SO4301 |
| A | HOH400 |
| A | HOH402 |
| A | HOH417 |
| A | HOH438 |
| A | HOH470 |
| A | HOH480 |
| C | HOH185 |
| C | HOH206 |
| C | HOH207 |
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 |
