p300 KAT domain in complex with KB528. Determined by X-ray diffraction at 2.0 Å resolution. Released 23 Jul 2025.
Explore 9IT5 in 3D Show helices and sheets RCSB PDB PDBe
9IT5 contains 47 α-helices and 20 β-strands across 2 chains. 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 | 1290-1292 | 3 | |
| α-helix | 1294-1295 | 2 | |
| α-helix | 1297-1313 | 17 | |
| β-strand | 1321-1334 | 14 | 1 |
| α-helix | 1335-1336 | 2 | |
| α-helix | 1337-1339 | 3 | |
| α-helix | 1340-1344 | 5 | |
| β-strand | 1352-1366 | 15 | 1 |
| β-strand | 1369-1381 | 13 | 1 |
| α-helix | 1386 | 1 | |
| β-strand | 1392-1400 | 9 | 1 |
| α-helix | 1407-1409 | 3 | |
| α-helix | 1410-1428 | 19 | |
| β-strand | 1432-1436 | 5 | 1 |
| α-helix | 1438-1440 | 3 | |
| β-strand | 1441 | 1 | 2 |
| β-strand | 1444 | 1 | 2 |
| α-helix | 1455-1459 | 5 | |
| α-helix | 1460-1476 | 17 | |
| β-strand | 1482-1485 | 4 | 1 |
| α-helix | 1486-1493 | 8 | |
| α-helix | 1498-1500 | 3 | |
| α-helix | 1508-1522 | 15 | |
| α-helix | 1558-1561 | 4 | |
| α-helix | 1579-1590 | 12 | |
| α-helix | 1592-1594 | 3 | |
| β-strand | 1595-1599 | 5 | 1 |
| α-helix | 1603-1607 | 5 | |
| α-helix | 1609-1612 | 4 | |
| α-helix | 1617-1618 | 2 | |
| β-strand | 1619 | 1 | 1 |
| α-helix | 1622-1624 | 3 | |
| α-helix | 1628-1636 | 9 | |
| α-helix | 1644-1660 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1290-1292 | 3 | |
| α-helix | 1294-1295 | 2 | |
| α-helix | 1297-1313 | 17 | |
| β-strand | 1321-1334 | 14 | 3 |
| α-helix | 1335-1336 | 2 | |
| α-helix | 1337-1339 | 3 | |
| α-helix | 1340-1344 | 5 | |
| β-strand | 1352-1365 | 14 | 3 |
| β-strand | 1370-1381 | 12 | 3 |
| α-helix | 1386 | 1 | |
| β-strand | 1392-1400 | 9 | 3 |
| α-helix | 1407-1409 | 3 | |
| α-helix | 1410-1428 | 19 | |
| β-strand | 1432-1436 | 5 | 3 |
| β-strand | 1441 | 1 | 4 |
| β-strand | 1444 | 1 | 4 |
| α-helix | 1455-1459 | 5 | |
| α-helix | 1460-1476 | 17 | |
| β-strand | 1482-1485 | 4 | 3 |
| α-helix | 1486-1492 | 7 | |
| α-helix | 1498-1500 | 3 | |
| α-helix | 1508-1521 | 14 | |
| α-helix | 1558-1560 | 3 | |
| α-helix | 1576-1590 | 15 | |
| α-helix | 1592-1594 | 3 | |
| β-strand | 1595-1599 | 5 | 3 |
| α-helix | 1603-1607 | 5 | |
| α-helix | 1609-1612 | 4 | |
| α-helix | 1617-1618 | 2 | |
| β-strand | 1619 | 1 | 3 |
| α-helix | 1622-1624 | 3 | |
| α-helix | 1628-1636 | 9 | |
| α-helix | 1644-1659 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone acetyltransferase p300 | A, B | protein | 349 | Homo sapiens | Q09472 (AlphaFold model) |
>9IT5_1 Histone acetyltransferase p300 (chains A, B) MKFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEVKPGMKARFVD SGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDSVHFFR PKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQE WYKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQKTS KNKSSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDP LIPCDLMDGRDAFLTLARDRHLEFSSLRRAQWSTGCMLVELHTQSQDRF
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1L3B | 4-[(2~{S})-1-[[(~{R})-[(3~{S})-7-(1-methylpyrazol-4-yl)-2,3-dihydro-1~{H}-pyrid… | C28 H28 N6 O | 2 |
Water and common crystallization additives (EDO, GOL, CL) are not listed.
Catalytic Inhibition of p300 Preferentially Targets IRF4 Oncogenic Activity and Tumor Growth in Multiple Myeloma. Lenoir, W.F., McKeown, M.R., Giorgetti, G. et al. Cancer Res (2026) 86:1010-1034. DOI 10.1158/0008-5472.CAN-25-3440 · PubMed
Other PDB entries of the same protein (UniProt Q09472 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 9IT5 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.