2F0Y
Crystal Structure Of Human Protein Farnesyltransferase Complexed With Farnesyl Diphosphate and hydantoin derivative
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004659 | molecular_function | prenyltransferase activity |
| A | 0004660 | molecular_function | protein farnesyltransferase activity |
| A | 0004661 | molecular_function | protein geranylgeranyltransferase activity |
| A | 0004662 | molecular_function | CAAX-protein geranylgeranyltransferase activity |
| A | 0004663 | molecular_function | Rab geranylgeranyltransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005875 | cellular_component | microtubule associated complex |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005953 | cellular_component | CAAX-protein geranylgeranyltransferase complex |
| A | 0005965 | cellular_component | protein farnesyltransferase complex |
| A | 0007167 | biological_process | enzyme-linked receptor protein signaling pathway |
| A | 0007179 | biological_process | transforming growth factor beta receptor signaling pathway |
| A | 0007323 | biological_process | peptide pheromone maturation |
| A | 0007528 | biological_process | neuromuscular junction development |
| A | 0008017 | molecular_function | microtubule binding |
| A | 0008318 | molecular_function | protein prenyltransferase activity |
| A | 0010698 | molecular_function | acetyltransferase activator activity |
| A | 0016601 | biological_process | Rac protein signal transduction |
| A | 0016740 | molecular_function | transferase activity |
| A | 0018342 | biological_process | protein prenylation |
| A | 0018343 | biological_process | protein farnesylation |
| A | 0018344 | biological_process | protein geranylgeranylation |
| A | 0019899 | molecular_function | enzyme binding |
| A | 0030971 | molecular_function | receptor tyrosine kinase binding |
| A | 0035022 | biological_process | positive regulation of Rac protein signal transduction |
| A | 0043014 | molecular_function | alpha-tubulin binding |
| A | 0060090 | molecular_function | molecular adaptor activity |
| A | 0060632 | biological_process | regulation of microtubule-based movement |
| A | 0071340 | biological_process | skeletal muscle acetylcholine-gated channel clustering |
| A | 1904395 | biological_process | positive regulation of skeletal muscle acetylcholine-gated channel clustering |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004659 | molecular_function | prenyltransferase activity |
| B | 0004660 | molecular_function | protein farnesyltransferase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| 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 | 0008284 | biological_process | positive 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 | 0042277 | molecular_function | peptide binding |
| B | 0045787 | biological_process | positive regulation of cell cycle |
| B | 0046872 | molecular_function | metal ion binding |
| 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 501 |
| Chain | Residue |
| B | ASP297 |
| B | CYS299 |
| B | HIS362 |
| B | 3MN963 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE FPP B 1001 |
| Chain | Residue |
| B | GLY250 |
| B | TYR251 |
| B | CYS254 |
| B | ARG291 |
| B | LYS294 |
| B | TYR300 |
| B | TRP303 |
| B | 3MN963 |
| B | HOH1011 |
| B | HOH1014 |
| B | HOH1024 |
| B | HOH1142 |
| B | HOH1186 |
| A | LYS164 |
| A | TYR166 |
| A | HIS201 |
| B | ARG202 |
| B | HIS248 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 3MN B 963 |
| Chain | Residue |
| B | TYR93 |
| B | LEU96 |
| B | SER99 |
| B | TRP102 |
| B | ASP297 |
| B | TYR300 |
| B | ASP359 |
| B | PHE360 |
| B | TYR361 |
| B | ZN501 |
| 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 | 33 |
| Details | Repeat: {"description":"PFTA 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 34 |
| Details | Repeat: {"description":"PFTA 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 33 |
| 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: {"evidences":[{"source":"PubMed","id":"11687658","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12036349","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12825937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15451670","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16893176","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11687658","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12036349","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12825937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15451670","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16893176","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19246009","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":"PubMed","id":"16893176","evidenceCode":"ECO:0000269"}]} |
| 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 |
