3Q35
Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A | Histone acetyltransferase | polymer | 438 | 50349.0 | 1 | UniProt (Q07794) Pfam (PF08214) In PDB | Saccharomyces cerevisiae (brewer's yeast lager beer yeast yeast) | Regulator of Ty1 transposition protein 109 |
2 | B | Vacuolar protein sorting-associated protein 75 | polymer | 232 | 27292.6 | 1 | UniProt (P53853) Pfam (PF00956) In PDB | Saccharomyces cerevisiae (brewer's yeast lager beer yeast yeast) | |
3 | A | ACETYL COENZYME *A | non-polymer | 809.6 | 1 | Chemie (ACO) | |||
4 | A | 1,2-ETHANEDIOL | non-polymer | 62.1 | 1 | Chemie (EDO) | |||
5 | water | water | 18.0 | 11 | Chemie (HOH) |
Sequence modifications
A: 1 - 436 (UniProt: Q07794)
PDB | External Database | Details |
---|---|---|
Gly -1 | - | expression tag |
Ser 0 | - | expression tag |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 2 |
Total formula weight | 77641.6 | |
Non-Polymers* | Number of molecules | 2 |
Total formula weight | 871.6 | |
All* | Total formula weight | 78513.2 |