1MZC
Co-Crystal Structure Of Human Farnesyltransferase With Farnesyldiphosphate and Inhibitor Compound 33a
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | Protein Farnesyltransferase alpha Subunit | polymer | 382 | 44864.8 | 1 | UniProt (P49354) Pfam (PF01239) | Homo sapiens (human) | CAAX farnesyltransferase alpha subunit, RAS proteins prenyltransferase alpha, FTase-alpha |
| 2 | B (B) | Protein Farnesyltransferase beta Subunit | polymer | 437 | 48822.4 | 1 | UniProt (P49356) Pfam (PF00432) | Homo sapiens (human) | CAAX farnesyltransferase beta subunit, RAS proteins prenyltransferase beta, FTase-beta |
| 3 | C (C) | beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose | branched | 342.3 | 1 | In PDB BIRD (PRD_900003) | sucrose | ||
| 4 | D (B) | ZINC ION | non-polymer | 65.4 | 1 | Chemie (ZN) | |||
| 5 | E (B) | FARNESYL DIPHOSPHATE | non-polymer | 382.3 | 1 | Chemie (FPP) | |||
| 6 | F (B) | 2-[3-(3-ETHYL-1-METHYL-2-OXO-AZEPAN-3-YL)-PHENOXY]-4-[1-AMINO-1-(1-METHYL-1H-IMIDIZOL-5-YL)-ETHYL]-BENZONITRILE | non-polymer | 471.6 | 1 | Chemie (BNE) | |||
| 7 | G, H (A, B) | water | water | 18.0 | 703 | Chemie (HOH) |
Sequence modifications
A: 1 - 379 (UniProt: P49354)
| PDB | External Database | Details |
|---|---|---|
| Glu 380 | - | cloning artifact |
| Glu 381 | - | cloning artifact |
| Phe 382 | - | cloning artifact |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 93687.2 | |
| Branched | Number of molecules | 1 |
| Total formula weight | 342.3 | |
| Non-Polymers* | Number of molecules | 3 |
| Total formula weight | 919.3 | |
| All* | Total formula weight | 94948.9 |
