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6V8K

Crystal structure of the p300 acetyltransferase domain with peptide-competitive inhibitor 2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004402molecular_functionhistone acetyltransferase activity
A0006355biological_processregulation of DNA-templated transcription
Functional Information from PDB Data
site_idAC1
Number of Residues22
Detailsbinding site for residue COA A 1701
ChainResidue
ALEU1398
AILE1457
APRO1458
AARG1462
ATRP1466
AHOH1801
AHOH1809
AHOH1811
AHOH1823
AHOH1826
AHOH1831
AASP1399
AHOH1837
AHOH1863
AHOH1875
ASER1400
AARG1410
ATHR1411
ATYR1414
ACYS1438
APRO1440
ALYS1456

site_idAC2
Number of Residues9
Detailsbinding site for residue QS4 A 1702
ChainResidue
AGLN1379
ATYR1394
AILE1395
ASER1396
ATYR1397
ATRP1436
ATYR1446
AGLU1505
AGLY1506

site_idAC3
Number of Residues4
Detailsbinding site for residue DMS A 1703
ChainResidue
ATRP1436
APHE1508
AHIS1591
AVAL1594

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsRegion: {"description":"Interaction with histone","evidences":[{"source":"PubMed","id":"18273021","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24819397","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"17065153","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"15004546","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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