1ygh Summary



The structure was published by Trievel, R.C., Rojas, J.R., Sterner, D.E., et al., Allis, C.D., Berger, S.L., and Marmorstein, R., in 1999 in a paper entitled "Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 1999.

The experimental data on which the structure is based was not deposited.

This PDB entry contains multiple copies of the structure of PROTEIN (TRANSCRIPTIONAL ACTIVATOR GCN5).

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 most likely forms homodimers.

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 PROTEIN (TRANSCRIPTIONAL ACTIVATOR GCN5) Q03330 (99-262) (GCN5_YEAST)search Saccharomyces cerevisiae S288csearch < 90% 164 100%
B PROTEIN (TRANSCRIPTIONAL ACTIVATOR GCN5) Q03330 (99-262) (GCN5_YEAST)search Saccharomyces cerevisiae S288csearch < 90% 164 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q03330 (99 - 262) PROTEIN (TRANSCRIPTIONAL ACTIVATOR GCN5) Saccharomyces cerevisiae

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B N-acetyl transferase, NATsearch Aminopeptidasesearch Acetyltransferase (GNAT) familysearch

Chain ID Molecular function (GO)
A, B (Q03330) N-acetyltransferase activitysearch

Chain InterPro annotation
A, B GNAT domainsearch Acyl-CoA N-acyltransferasesearch