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3Q33

Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated Histone Acetylation

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A
(A)
Histone acetyltransferase RTT109polymer43850349.01UniProt (Q07794)
Pfam (PF08214)
Saccharomyces cerevisiae (brewer's yeast lager beer yeast yeast)Regulator of Ty1 transposition protein 109
2B
(B)
Vacuolar protein sorting-associated protein 75polymer23227292.61UniProt (P53853)
Pfam (PF00956)
Saccharomyces cerevisiae (brewer's yeast lager beer yeast yeast)
3C
(D)
HISTONE H3polymer151492.71UniProt (P61830)synthetic
4D
(A)
ACETYL COENZYME *Anon-polymer809.61Chemie (ACO)
5E
(A)
1,2-ETHANEDIOLnon-polymer62.11Chemie (EDO)
6F, G
(A, B)
waterwater18.023Chemie (HOH)
Sequence modifications
A: 1 - 436 (UniProt: Q07794)
PDBExternal DatabaseDetails
Gly -1-expression tag
Ser 0-expression tag
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains3
Total formula weight79134.3
Non-Polymers*Number of molecules2
Total formula weight871.6
All*Total formula weight80005.9
*Water molecules are not included.

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PDB entries from 2026-02-25

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