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Ligands
Code Name Style Show Link
CMC Carboxymethyl coenzyme *a
Non-standard Residues
Code Name Show
ALY N(6)-acetyllysine
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 3TO6   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE/TRANSFERASE INHIBITOR
Title : Crystal structure of yeast Esa1 HAT domain complexed with H4K16CoA bisubstrate inhibitor
Release Data : 2011-11-09
Compound :
mol_id molecule chains
1 Histone acetyltransferase ESA1 A
ec: 2.3.1.48
fragment: UNP residues 160-435
mol_id molecule chains synonym
2 Histone H4 B K16CoA bisubstrate inhibitor
fragment: UNP residues 12-23
Source :
mol_id organism_scientific organism_common expression_system
1 Saccharomyces cerevisiae  (taxid:4932) Baker's yeast Escherichia coli  (taxid:562)
gene: ESA1, YOR244W, O5257
mol_id organism_scientific organism_common
2 Saccharomyces cerevisiae  (taxid:4932) Baker's yeast
synthetic: yes
Authors : Yuan, H., Ding, E.C., Marmorstein, R.
Keywords : acetyltransferase, autoacetylation, TRANSFERASE-TRANSFERASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 2.100 Å )
Citation :

MYST protein acetyltransferase activity requires active site lysine autoacetylation.

Yuan, H.,Rossetto, D.,Mellert, H.  et al.
(2011)  Embo J.  31 : 58 - 70

PubMed: 22020126
DOI: 10.1038/emboj.2011.382

Chain : A
UniProt : Q08649 (ESA1_YEAST)
Reaction: EC: Evidence:
Physiological Direction:
acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L- lysyl-[histone] 2.3.1.48 PubMed:12368900, PubMed:17223684, PubMed:18245364, PubMed:22020126, PubMed:9520405
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acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- lysyl-[protein] - PubMed:22539722, PubMed:29765047
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2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein] - UniProtKB:O94446
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(2E)-butenoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)- (2E)-butenoyl-L-lysyl-[protein] - PubMed:31699900
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Chain : B
UniProt : P02309 (H4_YEAST)
Reaction : -