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 | S.cerevisiae chromosome XVI reading frame ORF YPL253c | polymer | 298 | 34632.5 | 1 | UniProt (Q12045) Pfam (PF16796) In PDB | Saccharomyces cerevisiae (baker's yeast) | |
2 | A | 1,2-ETHANEDIOL | non-polymer | 62.1 | 1 | Chemie (EDO) | |||
3 | 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 |