4LNB
Aspergillus fumigatus protein farnesyltransferase ternary complex with farnesyldiphosphate and ethylenediamine scaffold inhibitor 5
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 | 0005737 | cellular_component | cytoplasm |
| A | 0005953 | cellular_component | CAAX-protein geranylgeranyltransferase complex |
| A | 0005965 | cellular_component | protein farnesyltransferase complex |
| A | 0007323 | biological_process | peptide pheromone maturation |
| A | 0008318 | molecular_function | protein prenyltransferase activity |
| A | 0018342 | biological_process | protein prenylation |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004659 | molecular_function | prenyltransferase activity |
| B | 0004660 | molecular_function | protein farnesyltransferase activity |
| B | 0005965 | cellular_component | protein farnesyltransferase complex |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008318 | molecular_function | protein prenyltransferase activity |
| B | 0018343 | biological_process | protein farnesylation |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0097354 | biological_process | prenylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 401 |
| Chain | Residue |
| A | ASP143 |
| A | SER146 |
| A | TYR147 |
| A | HIS148 |
| A | HOH717 |
| B | ARG381 |
| B | FPP601 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 402 |
| Chain | Residue |
| A | ARG47 |
| A | EDO403 |
| A | HOH567 |
| B | ASP170 |
| B | HOH782 |
| A | TYR35 |
| A | THR43 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 403 |
| Chain | Residue |
| A | THR43 |
| A | LEU46 |
| A | ARG47 |
| A | MET50 |
| A | HIS73 |
| A | EDO402 |
| B | HIS216 |
| B | GLY217 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE FPP B 601 |
| Chain | Residue |
| A | TYR147 |
| A | EDO401 |
| B | ARG274 |
| B | HIS333 |
| B | ALA335 |
| B | CYS339 |
| B | ARG381 |
| B | LYS384 |
| B | TYR390 |
| B | TRP393 |
| B | TYR454 |
| B | ED5603 |
| B | HOH704 |
| B | HOH714 |
| B | HOH718 |
| B | HOH737 |
| B | HOH830 |
| B | HOH971 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 602 |
| Chain | Residue |
| B | ASP387 |
| B | CYS389 |
| B | HIS455 |
| B | ED5603 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ED5 B 603 |
| Chain | Residue |
| B | ALA168 |
| B | SER172 |
| B | ARG274 |
| B | ASP387 |
| B | CYS389 |
| B | TYR390 |
| B | ASP452 |
| B | TYR454 |
| B | HIS455 |
| B | FPP601 |
| B | ZN602 |
| B | HOH820 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 604 |
| Chain | Residue |
| B | TYR154 |
| B | MET176 |
| B | TRP179 |
| B | ASP452 |
| B | SER453 |
| B | TYR454 |
| B | HOH813 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 605 |
| Chain | Residue |
| B | ALA171 |
| B | TRP175 |
| B | SER224 |
| B | HOH1004 |
