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HISTONE ACETYLTRANSFERASE HAT1 FROM SACCHAROMYCES CEREVISIAE IN COMPLEX WITH ACETYL COENZYME A

The structure was published by Dutnall, R.N., Tafrov, S.T., Sternglanz, R., and Ramakrishnan, V., in 1998 in a paper entitled "Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 1998.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of HISTONE ACETYLTRANSFERASE. This molecule has the UniProt identifier Q12341 (HAT1_YEAST)search. The sample contained 320 residues which is < 90% of the natural sequence. Out of 320 residues 303 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A HISTONE ACETYLTRANSFERASE Q12341 (1-320) (HAT1_YEAST)search Saccharomyces cerevisiae S288csearch < 90% 320 95%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q12341 (1 - 320) HISTONE ACETYLTRANSFERASE Saccharomyces cerevisiae

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A N-acetyl transferase, NATsearch Histone Acetyltransferase; Domain 1search, Aminopeptidasesearch, Arc Repressor Mutant, subunit Asearch Histone acetyl transferase HAT1 N-terminussearch, Acetyltransferase (GNAT) domainsearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (Q12341) histone acetyltransferase activitysearch histone bindingsearch N-acetyltransferase activitysearch chromatin modificationsearch chromatin silencing at telomeresearch histone acetylationsearch histone acetyltransferase complexsearch nucleussearch

Chain InterPro annotation
A GNAT domainsearch Histone acetyltransferase HAT1, C-terminalsearch Acyl-CoA N-acyltransferasesearch Histone acetyltransferase type B, catalytic subunitsearch Histone acetyl transferase HAT1 N-terminalsearch