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). 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):
This entry contains 1 unique UniProt protein: