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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 Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:24819397
ChainResidueDetails
ALEU1398
AARG1410
AILE1457
AARG1462
ATRP1466

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17065153
ChainResidueDetails
ALYS1336
ALYS1473

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:15004546
ChainResidueDetails
ALYS1499

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS1583

218853

PDB entries from 2024-04-24

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