Crystal structure of the p300 acetyltransferase catalytic core with butyryl-coenzyme A. Determined by X-ray diffraction at 2.04 Å resolution. Released 2 Nov 2016.
Explore 5LKT in 3D Show helices and sheets RCSB PDB PDBe
5LKT contains 36 α-helices and 19 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1051-1066 | 16 | |
| α-helix | 1073-1075 | 3 | |
| α-helix | 1089-1092 | 4 | |
| α-helix | 1099-1107 | 9 | |
| α-helix | 1114-1131 | 18 | |
| α-helix | 1137-1159 | 23 | |
| β-strand | 1169 | 1 | 1 |
| α-helix | 1170-1174 | 5 | |
| β-strand | 1175-1176 | 2 | 2 |
| β-strand | 1184-1185 | 2 | 2 |
| β-strand | 1190-1194 | 5 | 3 |
| β-strand | 1198-1201 | 4 | 3 |
| α-helix | 1202-1207 | 6 | |
| β-strand | 1212-1215 | 4 | 4 |
| β-strand | 1224-1227 | 4 | 4 |
| α-helix | 1228-1230 | 3 | |
| β-strand | 1232-1235 | 4 | 3 |
| α-helix | 1240 | 1 | |
| β-strand | 1241 | 1 | 1 |
| α-helix | 1242-1243 | 2 | |
| β-strand | 1244-1246 | 3 | 5 |
| β-strand | 1253-1255 | 3 | 5 |
| α-helix | 1256-1259 | 4 | |
| α-helix | 1273-1278 | 6 | |
| α-helix | 1283-1285 | 3 | |
| α-helix | 1294-1295 | 2 | |
| α-helix | 1297-1313 | 17 | |
| β-strand | 1321-1334 | 14 | 6 |
| α-helix | 1335-1336 | 2 | |
| α-helix | 1337-1339 | 3 | |
| α-helix | 1340-1344 | 5 | |
| β-strand | 1352-1366 | 15 | 6 |
| β-strand | 1369-1381 | 13 | 6 |
| α-helix | 1386 | 1 | |
| β-strand | 1392-1400 | 9 | 6 |
| α-helix | 1407-1409 | 3 | |
| α-helix | 1410-1428 | 19 | |
| β-strand | 1432-1436 | 5 | 6 |
| α-helix | 1439-1441 | 3 | |
| α-helix | 1456-1459 | 4 | |
| α-helix | 1460-1476 | 17 | |
| β-strand | 1482-1485 | 4 | 6 |
| α-helix | 1486-1492 | 7 | |
| α-helix | 1498-1500 | 3 | |
| α-helix | 1508-1519 | 12 | |
| α-helix | 1584-1590 | 7 | |
| α-helix | 1592-1594 | 3 | |
| β-strand | 1595-1599 | 5 | 6 |
| α-helix | 1603-1607 | 5 | |
| α-helix | 1609-1612 | 4 | |
| α-helix | 1617-1618 | 2 | |
| β-strand | 1619 | 1 | 6 |
| α-helix | 1622-1624 | 3 | |
| α-helix | 1628-1636 | 9 | |
| α-helix | 1644-1661 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone acetyltransferase p300,Histone acetyltransferase p300 | A | protein | 578 | Homo sapiens | Q09472 (AlphaFold model) |
>5LKT_1 Histone acetyltransferase p300,Histone acetyltransferase p300 (chains A) GAMAGKAVPMQSKKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDI VKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQE IDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHFCEKCFNEIQGES VSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVLHHEIIWPAGFVC DGCLKKSARTRKENKFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKT VEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRR VYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHP PDQKIPKPKRLQEWFKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKELPYFEGDFWPNV LEESIKESGGSGSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDPLIPCDLMDGRD AFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRF
Water and common crystallization additives (CL, DMS, GOL) are not listed.
Structure of p300 in complex with acyl-CoA variants. Kaczmarska, Z., Ortega, E., Goudarzi, A. et al. Nat Chem Biol (2017) 13:21-29. DOI 10.1038/nchembio.2217 · PubMed
Other PDB entries of the same protein (UniProt Q09472 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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