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5LKX

Crystal structure of the p300 acetyltransferase catalytic core with propionyl-coenzyme A.

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 Residues4
Detailsbinding site for residue ZN A 1701
ChainResidue
ACYS1177
ACYS1183
ACYS1201
ACYS1204

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
ACYS1164
AHIS1255
ACYS1258
ACYS1163

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN A 1704
ChainResidue
AHIS1315
AHIS1315
ACYS1408
ACYS1408

site_idAC5
Number of Residues24
Detailsbinding site for residue 1VU A 1705
ChainResidue
ASER1396
ALEU1398
AASP1399
ASER1400
ALYS1407
AARG1410
ATHR1411
ATYR1414
ATRP1436
ACYS1438
APRO1440
ATYR1446
ALYS1456
AILE1457
APRO1458
AARG1462
ALEU1463
ATRP1466
AHOH1807
AHOH1821
AHOH1833
AHOH1836
AHOH1864
AHOH1908

site_idAC6
Number of Residues8
Detailsbinding site for residue DMS A 1706
ChainResidue
AHIS1434
AILE1486
AASP1507
ATRP1509
APHE1595
APHE1596
AHOH1823
AHOH1899

site_idAC7
Number of Residues7
Detailsbinding site for residue GOL A 1707
ChainResidue
AILE1092
AVAL1093
ALYS1094
ASER1095
AASN1127
ALEU1130
AGLY1347

site_idAC8
Number of Residues5
Detailsbinding site for residue GOL A 1708
ChainResidue
ALYS1331
ATYR1355
ATHR1357
AGLN1379
ASER1396

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

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PDB entries from 2024-12-18

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