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6GYR

Transcription factor dimerization activates the p300 acetyltransferase

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
C0004402molecular_functionhistone acetyltransferase activity
C0006355biological_processregulation of DNA-templated transcription
D0004402molecular_functionhistone acetyltransferase activity
D0006355biological_processregulation of DNA-templated transcription
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 1701
ChainResidue
ACYS1163
ACYS1164
AHIS1255
ACYS1258

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 1702
ChainResidue
ACYS1247
ACYS1250
ACYS1272
ACYS1275

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 1703
ChainResidue
ACYS1183
ACYS1201
ACYS1204
ACYS1177

site_idAC4
Number of Residues17
Detailsbinding site for residue 01K A 1704
ChainResidue
ASER1396
ATYR1397
ALEU1398
AASP1399
ASER1400
AARG1410
ATHR1411
ATYR1414
ATRP1436
ACYS1438
APRO1440
ATYR1446
ALYS1456
AILE1457
APRO1458
AARG1462
ATRP1466

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN A 1705
ChainResidue
AHIS1315
ACYS1408
CHIS1315
CCYS1408

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN B 1701
ChainResidue
BCYS1163
BCYS1164
BHIS1255
BCYS1258

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN B 1702
ChainResidue
BCYS1247
BCYS1250
BCYS1272
BCYS1275

site_idAC8
Number of Residues5
Detailsbinding site for residue ZN B 1703
ChainResidue
BCYS1177
BGLY1179
BCYS1183
BCYS1201
BCYS1204

site_idAC9
Number of Residues19
Detailsbinding site for residue 01K B 1704
ChainResidue
BSER1396
BTYR1397
BLEU1398
BASP1399
BSER1400
BARG1410
BTHR1411
BTYR1414
BTRP1436
BCYS1438
BPRO1440
BASP1444
BTYR1446
BLYS1456
BILE1457
BPRO1458
BARG1462
BTRP1466
DLYS1407

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN B 1705
ChainResidue
BHIS1315
BCYS1408
DHIS1315
DCYS1408

site_idAD2
Number of Residues4
Detailsbinding site for residue ZN C 1701
ChainResidue
CCYS1163
CCYS1164
CHIS1255
CCYS1258

site_idAD3
Number of Residues4
Detailsbinding site for residue ZN C 1702
ChainResidue
CCYS1247
CCYS1250
CCYS1272
CCYS1275

site_idAD4
Number of Residues4
Detailsbinding site for residue ZN C 1703
ChainResidue
CCYS1177
CCYS1183
CCYS1201
CCYS1204

site_idAD5
Number of Residues20
Detailsbinding site for residue 01K C 1704
ChainResidue
CPHE1467
CARG1627
CSER1396
CTYR1397
CLEU1398
CASP1399
CSER1400
CLYS1407
CARG1410
CTHR1411
CTYR1414
CTRP1436
CPRO1440
CTYR1446
CLYS1456
CILE1457
CPRO1458
CARG1462
CLEU1463
CTRP1466

site_idAD6
Number of Residues4
Detailsbinding site for residue ZN D 1701
ChainResidue
DCYS1163
DCYS1164
DHIS1255
DCYS1258

site_idAD7
Number of Residues4
Detailsbinding site for residue ZN D 1702
ChainResidue
DCYS1247
DCYS1250
DCYS1272
DCYS1275

site_idAD8
Number of Residues4
Detailsbinding site for residue ZN D 1703
ChainResidue
DCYS1177
DCYS1183
DCYS1201
DCYS1204

site_idAD9
Number of Residues24
Detailsbinding site for residue 01K D 1704
ChainResidue
BLYS1407
DSER1396
DTYR1397
DLEU1398
DASP1399
DSER1400
DARG1410
DTHR1411
DTYR1414
DTRP1436
DALA1437
DCYS1438
DPRO1439
DPRO1440
DASP1444
DTYR1446
DGLN1455
DLYS1456
DILE1457
DPRO1458
DLYS1459
DARG1462
DTRP1466
DARG1627

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 Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:24819397
ChainResidueDetails
ALEU1398
BTRP1466
CLEU1398
CARG1410
CILE1457
CARG1462
CTRP1466
DLEU1398
DARG1410
DILE1457
DARG1462
AARG1410
DTRP1466
AILE1457
AARG1462
ATRP1466
BLEU1398
BARG1410
BILE1457
BARG1462

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:B2RWS6
ChainResidueDetails
ALYS1180
BLYS1180
CLYS1180
DLYS1180

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17065153
ChainResidueDetails
ALYS1336
ALYS1473
BLYS1336
BLYS1473
CLYS1336
CLYS1473
DLYS1336
DLYS1473

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:15004546
ChainResidueDetails
ALYS1499
BLYS1499
CLYS1499
DLYS1499

site_idSWS_FT_FI5
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18995842, ECO:0007744|PubMed:19608861
ChainResidueDetails
APRO1574
AASN1578
BPRO1574
BASN1578
CPRO1574
CASN1578
DPRO1574
DASN1578

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:15004546, ECO:0000269|PubMed:18995842
ChainResidueDetails
ASER1581
BSER1581
CSER1581
DSER1581

site_idSWS_FT_FI7
Number of Residues8
DetailsMOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:15004546, ECO:0007744|PubMed:19608861
ChainResidueDetails
AALA1586
ALYS1592
BALA1586
BLYS1592
CALA1586
CLYS1592
DALA1586
DLYS1592

site_idSWS_FT_FI8
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ATHR1587
APRO1615
BTHR1587
BPRO1615
CTHR1587
CPRO1615
DTHR1587
DPRO1615

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:15004546, ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS1590
BLYS1590
CLYS1590
DLYS1590

221716

PDB entries from 2024-06-26

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