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CRYSTAL STRUCTURE OF THE PCAF/COENZYME-A COMPLEX

The structure was published by Clements, A., Rojas, J.R., Trievel, R.C., Wang, L., Berger, S.L., and Marmorstein, R., in 1999 in a paper entitled "Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 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 P300/CBP ASSOCIATING FACTOR.

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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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
B P300/CBP ASSOCIATING FACTOR Q92831 (493-658) (KAT2B_HUMAN)search Homo sapienssearch < 90% 168 97%
A P300/CBP ASSOCIATING FACTOR Q92831 (493-658) (KAT2B_HUMAN)search Homo sapienssearch < 90% 168 97%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q92831 (493 - 658) P300/CBP ASSOCIATING FACTOR Homo sapiens

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

Chain ID Molecular function (GO)
B, A (Q92831) N-acetyltransferase activitysearch

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