2BED
Structure of FPT bound to inhibitor SCH207736
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008318 | molecular_function | protein prenyltransferase activity |
| A | 0018342 | biological_process | protein prenylation |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004311 | molecular_function | geranylgeranyl diphosphate synthase activity |
| B | 0004659 | molecular_function | prenyltransferase activity |
| B | 0004660 | molecular_function | protein farnesyltransferase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005875 | cellular_component | microtubule associated complex |
| B | 0005965 | cellular_component | protein farnesyltransferase complex |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008283 | biological_process | cell population proliferation |
| B | 0008284 | biological_process | positive regulation of cell population proliferation |
| B | 0008285 | biological_process | negative regulation of cell population proliferation |
| B | 0008318 | molecular_function | protein prenyltransferase activity |
| B | 0010698 | molecular_function | acetyltransferase activator activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0018343 | biological_process | protein farnesylation |
| B | 0019899 | molecular_function | enzyme binding |
| B | 0042060 | biological_process | wound healing |
| B | 0042277 | molecular_function | peptide binding |
| B | 0045787 | biological_process | positive regulation of cell cycle |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048144 | biological_process | fibroblast proliferation |
| B | 0048145 | biological_process | regulation of fibroblast proliferation |
| B | 0048146 | biological_process | positive regulation of fibroblast proliferation |
| B | 0060632 | biological_process | regulation of microtubule-based movement |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1 |
| Chain | Residue |
| B | ASP297 |
| B | CYS299 |
| B | HIS362 |
| B | 7362001 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE FPP B 1001 |
| Chain | Residue |
| B | TYR251 |
| B | CYS254 |
| B | ARG291 |
| B | LYS294 |
| B | TYR300 |
| B | TRP303 |
| B | 7362001 |
| A | LYS164 |
| A | TYR166 |
| B | TYR205 |
| B | HIS248 |
| B | GLY250 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 736 B 2001 |
| Chain | Residue |
| A | LYS164 |
| A | TYR166 |
| A | HIS201 |
| B | ZN1 |
| B | CYS95 |
| B | LEU96 |
| B | TRP102 |
| B | TRP106 |
| B | TYR300 |
| B | ASP359 |
| B | TYR361 |
| B | FPP1001 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 34 |
| Details | Repeat: {"description":"PFTA 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 34 |
| Details | Repeat: {"description":"PFTA 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 32 |
| Details | Repeat: {"description":"PFTA 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 34 |
| Details | Repeat: {"description":"PFTA 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 34 |
| Details | Repeat: {"description":"PFTA 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 41 |
| Details | Repeat: {"description":"PFTB 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 41 |
| Details | Repeat: {"description":"PFTB 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 41 |
| Details | Repeat: {"description":"PFTB 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 42 |
| Details | Repeat: {"description":"PFTB 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 42 |
| Details | Repeat: {"description":"PFTB 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 9 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18844669","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20056542","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9065406","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for selectivity against geranylgeranyl diphosphate","evidences":[{"source":"UniProtKB","id":"P49356","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1d8d |
| Chain | Residue | Details |
| A | LYS164 | |
| B | TYR300 |
| site_id | MCSA1 |
| Number of Residues | 9 |
| Details | M-CSA 484 |
| Chain | Residue | Details |
| B | HIS248 | electrostatic stabiliser |
| B | ARG291 | electrostatic stabiliser |
| B | LYS294 | electrostatic stabiliser |
| B | ASP297 | metal ligand |
| B | CYS299 | metal ligand |
| B | TYR300 | electrostatic stabiliser |
| B | ASP352 | metal ligand |
| B | ASP359 | electrostatic stabiliser |
| B | HIS362 | metal ligand |
