2O0A
The structure of the C-terminal domain of Vik1 has a motor domain fold but lacks a nucleotide-binding site.
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | S.cerevisiae chromosome XVI reading frame ORF YPL253c | polymer | 298 | 34632.5 | 1 | UniProt (Q12045) Pfam (PF16796) | Saccharomyces cerevisiae (baker's yeast) | |
| 2 | B (A) | 1,2-ETHANEDIOL | non-polymer | 62.1 | 1 | Chemie (EDO) | |||
| 3 | C (A) | water | water | 18.0 | 241 | Chemie (HOH) |
Sequence modifications
A: 353 - 647 (UniProt: Q12045)
| PDB | External Database | Details |
|---|---|---|
| Gly 350 | - | cloning artifact |
| Ala 351 | - | cloning artifact |
| Ser 352 | - | cloning artifact |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 34632.5 | |
| Non-Polymers* | Number of molecules | 1 |
| Total formula weight | 62.1 | |
| All* | Total formula weight | 34694.6 |
