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6K4N

Cryo-EM structure of p300

Replaces:  5XZS
Functional Information from GO Data
ChainGOidnamespacecontents
A0004402molecular_functionhistone acetyltransferase activity
A0006355biological_processregulation of DNA-templated transcription
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 Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:24819397
ChainResidueDetails
ALEU1398
AARG1410
AILE1457
AARG1462
ATRP1466

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:B2RWS6
ChainResidueDetails
ALYS1180

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17065153
ChainResidueDetails
ALYS1336
ALYS1473

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:15004546
ChainResidueDetails
ALYS1499

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18995842, ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS1542
ALYS1546

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:15004546, ECO:0000269|PubMed:18995842
ChainResidueDetails
ALYS1549

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:15004546, ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS1554
ALYS1560

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS1555
ALYS1583

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:15004546, ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS1558

223790

PDB entries from 2024-08-14

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