SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborDownloads>


Crystal structure of p300 histone acetyltransferase domain in complex with a bisubstrate inhibitor, Lys-CoA

Summary for 3BIY

DescriptorHistone acetyltransferase p300 (E.C.
Functional Keywordsp300 HAT, Bisubstrate inhibitor, protein-inhibitor complex, TRANSFERASE,TRANSFERASE
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm Q09472
Total number of polymer chains1
Total molecular weight45370.67
Liu, X.,Wang, L.,Zhao, K.,Thompson, P.R.,Hwang, Y.,Marmorstein, R.,Cole, P.A. (deposition date: 2007-12-02, release date: 2008-02-12, modification date: 2011-07-13)
Primary citation
Liu, X.,Wang, L.,Zhao, K.,Thompson, P.R.,Hwang, Y.,Marmorstein, R.,Cole, P.A.
The structural basis of protein acetylation by the p300/CBP transcriptional coactivator
Nature, 451:846-850, 2008
PubMed: 18273021
DOI: 10.1038/nature06546
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.212602.1%7.5%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

no rotation
rotated about x axis by 90°
rotated about y axis by 90°
Copyright © 2013-2015 Protein Data Bank Japan
  • Everything
  • PDBID/Keywords
  • Author
  • Chemie
  • Sequence
  • ?
entries available on 2015-07-01
00:00 UTC / 09:00 JST