Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T25956 | Target Info | |||
| Target Name | Histone acetyltransferase p300 (EP300) | ||||
| Synonyms | p300 HAT; Protein propionyltransferase p300; P300; Histone crotonyltransferase p300; Histone butyryltransferase p300; E1Aassociated protein p300; E1A-associated protein p300 | ||||
| Target Type | Clinical trial Target | ||||
| Gene Name | EP300 | ||||
| Biochemical Class | Acyltransferase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | [(2r,3s,4r,5r)-5-(6-Amino-9h-Purin-9-Yl)-4-Hydroxy-3-(Phosphonooxy)tetrahydrofuran-2-Yl]methyl (3r,20r)-20-Carbamoyl-3-Hydroxy-2,2-Dimethyl-4,8,14,22-Tetraoxo-12-Thia-5,9,15,21-Tetraazatricos-1-Yl Dihydrogen Diphosphate | Ligand Info | |||
| Canonical SMILES | CC(=O)NC(CCCCNC(=O)CSCCNC(=O)CCNC(=O)C(C(C)(C)COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)N2C=NC3=C(N=CN=C32)N)O)OP(=O)(O)O)O)C(=O)N | ||||
| InChI | 1S/C31H53N10O19P3S/c1-17(42)40-18(27(33)47)6-4-5-8-34-21(44)13-64-11-10-35-20(43)7-9-36-29(48)25(46)31(2,3)14-57-63(54,55)60-62(52,53)56-12-19-24(59-61(49,50)51)23(45)30(58-19)41-16-39-22-26(32)37-15-38-28(22)41/h15-16,18-19,23-25,30,45-46H,4-14H2,1-3H3,(H2,33,47)(H,34,44)(H,35,43)(H,36,48)(H,40,42)(H,52,53)(H,54,55)(H2,32,37,38)(H2,49,50,51)/t18-,19-,23-,24-,25+,30-/m1/s1 | ||||
| InChIKey | YGZKIOPJGFQDSR-VLHHDIFDSA-N | ||||
| PubChem Compound ID | 23727984 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 6GYR Transcription factor dimerization activates the p300 acetyltransferase | ||||||
| Method | X-ray diffraction | Resolution | 3.10 Å | Mutation | Yes | [1] |
| PDB Sequence |
AKKIFKPEEL
1054 RQALMPTLEA1064 LYRQDPESLP1074 FRQPVDPQLL1084 GIPDYFDIVK1094 SPMDLSTIKR 1104 KLDTGQYQEP1114 WQYVDDIWLM1124 FNNAWLYNRK1134 TSRVYKYCSK1144 LSEVFEQEID 1154 PVMQSLGYCC1164 GRKLEFSPQT1174 LCCYGKQLCT1184 IPRDATYYSY1194 QNRYHFCEKC 1204 FNEIQGESVS1214 LGDDPSQPQT1224 TINKEQFSKR1234 KNDTLDPELF1244 VECTECGRKM 1254 HQICVLHHEI1264 IWPAGFVCDG1274 CLKKSARTRK1284 ENKFSAKRLP1294 STRLGTFLEN 1304 RVNDFLRRQN1314 HPESGEVTVR1324 VVHASDKTVE1334 VKPGMKARFV1344 DSGEMAESFP 1354 YRTKALFAFE1364 EIDGVDLCFF1374 GMHVQEYGSD1384 CPPPNQRRVY1394 ISYLDSVHFF 1404 RPKCLRTAVY1414 HEILIGYLEY1424 VKKLGYTTGH1434 IWACPPSEGD1444 DYIFHCHPPD 1454 QKIPKPKRLQ1464 EWFKKMLDKA1474 VSERIVHDYK1484 DIFKQATEDR1494 LTSAKELPYF 1504 EGDFWPNVLE1514 ESIKELEQEE1524 EERKREENTG1566 NKKKPGMPNV1576 SNDLSQKLYA 1586 TMEKHKEVFF1596 VIRLIAGPAA1606 NSLPPIVDPD1616 PLIPCDLMDG1626 RDAFLTLARD 1636 KHLEFSSLRR1646 AQWSTMCMLV1656 ELHTQSQD
|
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|
|
PHE1374
3.641
TYR1394
3.990
ILE1395
3.897
SER1396
2.198
TYR1397
2.175
LEU1398
2.225
ASP1399
2.328
SER1400
1.692
LYS1407
3.440
ARG1410
2.005
THR1411
1.744
TYR1414
2.015
ILE1435
2.966
TRP1436
2.103
ALA1437
2.990
CYS1438
1.983
PRO1439
2.338
PRO1440
2.800
|
|||||
| PDB ID: 4BHW Structural basis for autoinhibition of the acetyltransferase activity of p300 | ||||||
| Method | X-ray diffraction | Resolution | 2.80 Å | Mutation | Yes | [2] |
| PDB Sequence |
KKIFKPEELR
1055 QALMPTLEAL1065 YRQDPESLPF1075 RQPVDPQLLG1085 IPDYFDIVKS1095 PMDLSTIKRK 1105 LDTGQYQEPW1115 QYVDDIWLMF1125 NNAWLYNRKT1135 SRVYKYCSKL1145 SEVFEQEIDP 1155 VMQSLGYCCG1165 RKLEFSPQTL1175 CCYGKQLCTI1185 PRDATYYSYQ1195 NRYHFCEKCF 1205 NEIQGESVSL1215 GDDPSQPQTT1225 INKEQFSKRK1235 NDTLDPELFV1245 ECTECGRKMH 1255 QICVLHHEII1265 WPAGFVCDGC1275 LKKSARTRKE1285 NKFSAKRLPS1295 TRLGTFLENR 1305 VNDFLRRQNH1315 PESGEVTVRV1325 VHASDKTVEV1335 KPGMKARFVD1345 SGEMAESFPY 1355 RTKALFAFEE1365 IDGVDLCFFG1375 MHVQEYGSDC1385 PPPNQRRVYI1395 SYLDSVHFFR 1405 PKCLRTAVYH1415 EILIGYLEYV1425 KKLGYTTGHI1435 WACPPSEGDD1445 YIFHCHPPDQ 1455 KIPKPKRLQE1465 WFKKMLDKAV1475 SERIVHDYKD1485 IFKQATEDRL1495 TSAKELPYFE 1505 GDFWPNVLEE1515 SIKESGGSGS1581 QKLYATMEKH1591 KEVFFVIRLI1601 AGPAANSLPP 1611 IVDPDPLIPC1621 DLMDGRDAFL1631 TLARDKHLEF1641 SSLRRAQWST1651 MCMLVELHTQ 1661 SQD
|
|||||
|
|
PHE1374
4.873
ILE1395
4.711
SER1396
3.169
TYR1397
2.493
LEU1398
2.896
ASP1399
3.348
SER1400
2.451
LYS1407
3.650
ARG1410
2.928
THR1411
3.000
TYR1414
3.302
ILE1435
4.190
TRP1436
2.784
ALA1437
3.777
CYS1438
3.696
PRO1439
4.122
|
|||||
| PDB ID: 3BIY Crystal structure of p300 histone acetyltransferase domain in complex with a bisubstrate inhibitor, Lys-CoA | ||||||
| Method | X-ray diffraction | Resolution | 1.70 Å | Mutation | Yes | [3] |
| PDB Sequence |
KFSAKRLPST
1296 RLGTFLENRV1306 NDFLRRQNHP1316 ESGEVTVRVV1326 HASDKTVEVK1336 PGMKARFVDS 1346 GEMAESFPYR1356 TKALFAFEEI1366 DGVDLCFFGM1376 HVQEYGSDCP1386 PPNQRRVYIS 1396 YLDSVHFFRP1406 KCLRTAVYHE1416 ILIGYLEYVK1426 KLGYTTGHIW1436 ACPPSEGDDY 1446 IFHCHPPDQK1456 IPKPKRLQEW1466 YKKMLDKAVS1476 ERIVHDYKDI1486 FKQATEDRLT 1496 SAKELPYFEG1506 DFWPNVLEES1516 IKESQKLYAT1587 MEKHKEVFFV1597 IRLIAGPAAN 1607 SLPPIVDPDP1617 LIPCDLMDGR1627 DAFLTLARDR1637 HLEFSSLRRA1647 QWSTGCMLVE 1657 LHTQSQD
|
|||||
|
|
ILE1395
4.325
SER1396
3.340
TYR1397
3.224
LEU1398
2.908
ASP1399
3.526
SER1400
2.617
LYS1407
4.557
ARG1410
2.891
THR1411
2.678
TYR1414
3.279
ILE1435
4.360
TRP1436
2.958
ALA1437
3.706
CYS1438
3.646
PRO1439
3.753
|
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Transcription factor dimerization activates the p300 acetyltransferase. Nature. 2018 Oct;562(7728):538-544. | ||||
| REF 2 | Structure of the p300 catalytic core and implications for chromatin targeting and HAT regulation. Nat Struct Mol Biol. 2013 Sep;20(9):1040-6. | ||||
| REF 3 | The structural basis of protein acetylation by the p300/CBP transcriptional coactivator. Nature. 2008 Feb 14;451(7180):846-50. | ||||
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