1D8D
CO-CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A K-RAS4B PEPTIDE SUBSTRATE AND FPP ANALOG AT 2.0A RESOLUTION
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 | 0005875 | cellular_component | microtubule associated complex |
| A | 0005953 | cellular_component | CAAX-protein geranylgeranyltransferase complex |
| A | 0005965 | cellular_component | protein farnesyltransferase complex |
| A | 0006998 | biological_process | nuclear envelope organization |
| A | 0007167 | biological_process | enzyme-linked receptor protein signaling pathway |
| A | 0007323 | biological_process | peptide pheromone maturation |
| A | 0008017 | molecular_function | microtubule binding |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008284 | biological_process | positive regulation of cell population proliferation |
| A | 0008318 | molecular_function | protein prenyltransferase activity |
| A | 0010698 | molecular_function | acetyltransferase activator activity |
| 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 | 0036094 | molecular_function | small molecule binding |
| A | 0042277 | molecular_function | peptide binding |
| A | 0043014 | molecular_function | alpha-tubulin binding |
| A | 0043066 | biological_process | negative regulation of apoptotic process |
| A | 0045787 | biological_process | positive regulation of cell cycle |
| A | 0051604 | biological_process | protein maturation |
| A | 0060090 | molecular_function | molecular adaptor activity |
| A | 0060632 | biological_process | regulation of microtubule-based movement |
| A | 1901363 | molecular_function | heterocyclic compound binding |
| A | 1904395 | biological_process | positive regulation of skeletal muscle acetylcholine-gated channel clustering |
| 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 | 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 | 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 | 9 |
| Details | BINDING SITE FOR RESIDUE ACT P 3000 |
| Chain | Residue |
| B | TYR93 |
| B | CYS95 |
| B | LEU96 |
| B | ASP359 |
| P | LYS3 |
| P | LYS7 |
| P | HOH1166 |
| P | HOH1330 |
| P | ACT3001 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT P 3001 |
| Chain | Residue |
| B | LEU96 |
| B | TYR361 |
| P | LYS3 |
| P | CYS8 |
| P | HOH1246 |
| P | HOH1318 |
| P | ACT3000 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 3002 |
| Chain | Residue |
| B | LEU89 |
| B | THR90 |
| B | TYR93 |
| B | HOH1183 |
| B | HOH1449 |
| B | ACT3003 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 3003 |
| Chain | Residue |
| B | TYR81 |
| B | TYR93 |
| B | ARG358 |
| B | ASP359 |
| B | HOH1449 |
| B | ACT3002 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1001 |
| Chain | Residue |
| B | ASP297 |
| B | CYS299 |
| B | HIS362 |
| P | CYS8 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE FII B 1000 |
| Chain | Residue |
| A | LYS164 |
| A | TYR166 |
| B | HIS248 |
| B | GLY250 |
| B | CYS254 |
| B | ARG291 |
| B | LYS294 |
| B | TYR300 |
| B | TRP303 |
| B | HOH1162 |
| B | HOH1164 |
| B | HOH1165 |
| B | HOH1168 |
| B | HOH1198 |
| B | HOH1253 |
| P | ILE10 |
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 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Propeptide: {"description":"Removed in mature form","featureId":"PRO_0000281291","evidences":[{"source":"PubMed","id":"27791178","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Cysteine methyl ester","evidences":[{"source":"PubMed","id":"27791178","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5TAR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5TB5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 1 |
| Details | Lipidation: {"description":"N6-palmitoyl lysine","evidences":[{"source":"PubMed","id":"29239724","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 1 |
| Details | Lipidation: {"description":"S-farnesyl cysteine","evidences":[{"source":"PubMed","id":"27791178","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24415755","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5TAR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5TB5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| 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 |
