9IT5: P300 KAT domain

p300 KAT domain in complex with KB528. Determined by X-ray diffraction at 2.0 Å resolution. Released 23 Jul 2025.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
2
Atoms
6,007
Mol. weight
82.09 kDa
Ligands
A1L3B
Released
23 Jul 2025

Explore 9IT5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 24 helices, 10 β-strands

ElementResiduesLengthSheet
α-helix1290-12923
α-helix1294-12952
α-helix1297-131317
β-strand1321-1334141
α-helix1335-13362
α-helix1337-13393
α-helix1340-13445
β-strand1352-1366151
β-strand1369-1381131
α-helix13861
β-strand1392-140091
α-helix1407-14093
α-helix1410-142819
β-strand1432-143651
α-helix1438-14403
β-strand144112
β-strand144412
α-helix1455-14595
α-helix1460-147617
β-strand1482-148541
α-helix1486-14938
α-helix1498-15003
α-helix1508-152215
α-helix1558-15614
α-helix1579-159012
α-helix1592-15943
β-strand1595-159951
α-helix1603-16075
α-helix1609-16124
α-helix1617-16182
β-strand161911
α-helix1622-16243
α-helix1628-16369
α-helix1644-166017
Chain B: 23 helices, 10 β-strands
ElementResiduesLengthSheet
α-helix1290-12923
α-helix1294-12952
α-helix1297-131317
β-strand1321-1334143
α-helix1335-13362
α-helix1337-13393
α-helix1340-13445
β-strand1352-1365143
β-strand1370-1381123
α-helix13861
β-strand1392-140093
α-helix1407-14093
α-helix1410-142819
β-strand1432-143653
β-strand144114
β-strand144414
α-helix1455-14595
α-helix1460-147617
β-strand1482-148543
α-helix1486-14927
α-helix1498-15003
α-helix1508-152114
α-helix1558-15603
α-helix1576-159015
α-helix1592-15943
β-strand1595-159953
α-helix1603-16075
α-helix1609-16124
α-helix1617-16182
β-strand161913
α-helix1622-16243
α-helix1628-16369
α-helix1644-165916

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone acetyltransferase p300A, Bprotein349Homo sapiensQ09472 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>9IT5_1 Histone acetyltransferase p300 (chains A, B)
MKFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEVKPGMKARFVD
SGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDSVHFFR
PKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQE
WYKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQKTS
KNKSSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDP
LIPCDLMDGRDAFLTLARDRHLEFSSLRRAQWSTGCMLVELHTQSQDRF

Ligands and cofactors

IDNameFormulaCopies
A1L3B4-[(2~{S})-1-[[(~{R})-[(3~{S})-7-(1-methylpyrazol-4-yl)-2,3-dihydro-1~{H}-pyrid…C28 H28 N6 O2

Water and common crystallization additives (EDO, GOL, CL) are not listed.

Primary citation

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:

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