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6V90

Crystal structure of the p300 acetyltransferase domain with AcCoA competitive inhibitor 12

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 Residues14
Detailsbinding site for residue QSD A 1701
ChainResidue
ALEU1398
APRO1458
AARG1462
ALEU1463
ATRP1466
AHOH1825
AASP1399
ASER1400
APRO1440
AGLY1443
AASP1444
AHIS1451
AGLN1455
AILE1457

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 1702
ChainResidue
AALA1350
AGLU1351
ASER1352
AARG1462

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 1703
ChainResidue
AARG1478
AARG1478
AHIS1481

site_idAC4
Number of Residues5
Detailsbinding site for residue CL A 1704
ChainResidue
ALEU1398
ATYR1446
ALYS1558
AHOH1849
AHOH1853

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 Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18995842, ECO:0007744|PubMed:19608861
ChainResidueDetails
APRO1574
AASN1578

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:15004546, ECO:0000269|PubMed:18995842
ChainResidueDetails
ASER1581

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:15004546, ECO:0007744|PubMed:19608861
ChainResidueDetails
AALA1586
ALYS1592

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ATHR1587
APRO1615

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:15004546, ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS1590

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PDB entries from 2024-07-17

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