Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4BHW

Structural basis for autoinhibition of the acetyltransferase activity of p300

Functional Information from GO Data
ChainGOidnamespacecontents
A0004402molecular_functionhistone acetyltransferase activity
A0006355biological_processregulation of DNA-templated transcription
B0004402molecular_functionhistone acetyltransferase activity
B0006355biological_processregulation of DNA-templated transcription
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1
ChainResidue
ACYS1163
ACYS1164
AHIS1255
ACYS1258

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 2
ChainResidue
ACYS1247
ACYS1250
ACYS1272
ACYS1275

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 3
ChainResidue
ACYS1183
ACYS1201
ACYS1204
ACYS1177

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 4
ChainResidue
AHIS1315
ACYS1408
BHIS1315
BCYS1408

site_idAC5
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 01K A 700
ChainResidue
ASER1396
ATYR1397
ALEU1398
AASP1399
ASER1400
ALYS1407
AARG1410
ATHR1411
ATYR1414
ATRP1436
ACYS1438
APRO1440
ATYR1446
ALYS1456
AILE1457
APRO1458
AARG1462
ATRP1466
APHE1467
AHOH2003
BLYS1407

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1
ChainResidue
BCYS1163
BCYS1164
BHIS1255
BCYS1258

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 2
ChainResidue
BCYS1247
BCYS1250
BCYS1272
BCYS1275

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 3
ChainResidue
BCYS1177
BCYS1183
BCYS1201
BCYS1204

site_idAC9
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 01K B 700
ChainResidue
BSER1396
BTYR1397
BLEU1398
BASP1399
BSER1400
BARG1410
BTHR1411
BTYR1414
BTRP1436
BCYS1438
BPRO1440
BTYR1446
BLYS1456
BILE1457
BPRO1458
BARG1462
BTRP1466
BPHE1467

Functional Information from PROSITE/UniProt
site_idPS00633
Number of Residues60
DetailsBROMODOMAIN_1 Bromodomain signature. SlpFrqpvDpqllgipDYFdiVkspMdlstIkrkldtgq..Yqepwqyvddiwl.MfnNAwlY
ChainResidueDetails
ASER1072-TYR1131

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues214
DetailsDomain: {"description":"Bromo","evidences":[{"source":"PROSITE-ProRule","id":"PRU00035","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsRegion: {"description":"Interaction with histone","evidences":[{"source":"PubMed","id":"18273021","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24819397","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"B2RWS6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"17065153","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"15004546","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon