8Q5P: Lysine methyltransferase SETD2

Structure of the lysine methyltransferase SETD2 in complex with a peptide derived from human tyrosine kinase ACK1. Determined by X-ray diffraction at 1.81 Å resolution. Released 24 Apr 2024.

Method
X-ray diffraction
Resolution
1.81 Å
Organism
Homo sapiens
Chains
2
Atoms
2,256
Mol. weight
36.04 kDa
Ligands
SAM, ZN
Released
24 Apr 2024

Explore 8Q5P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8Q5P contains 16 α-helices and 23 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: 16 helices, 21 β-strands

ElementResiduesLengthSheet
β-strand1448-145031
α-helix1451-14544
α-helix1457-14659
α-helix1470-14723
β-strand1474-147522
β-strand1480-148123
α-helix1501-15055
α-helix1506-15116
α-helix1513-15142
α-helix1521-15244
β-strand152714
α-helix1536-15383
α-helix1543-15464
β-strand1552-155651
β-strand1562-156651
β-strand157015
β-strand1575-157844
β-strand1582-158433
α-helix1586-159914
β-strand1606-161053
β-strand1613-161643
β-strand1620-162122
α-helix1623-16264
α-helix16271
β-strand1628-162924
β-strand1635-164284
β-strand1645-165284
β-strand165615
α-helix16601
β-strand1661-166221
β-strand1663-166424
β-strand1669-167026
α-helix16751
β-strand1676-167727
α-helix16781
β-strand1688-168927
α-helix1697-17004
Chain B: 0 helices, 2 β-strands
ElementResiduesLengthSheet
β-strand34-3526
β-strand3613

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone-lysine N-methyltransferase SETD2Aprotein295Homo sapiensQ9BYW2 (AlphaFold model)
Activated CDC42 kinase 1Bprotein12Homo sapiensQ07912 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8Q5P_1 Histone-lysine N-methyltransferase SETD2 (chains A)
MHHHHHHSSGRENLYFQGETSVPPGSALVGPSCVMDDFRDPQRWKECAKQGKMPCYFDLI
EENVYLTERKKNKSHRDIKRMQCECTPLSKDERAQGEIACGEDCLNRLLMIECSSRCPNG
DYCSNRRFQRKQHADVEVILTEKKGWGLRAAKDLPSNTFVLEYCGEVLDHKEFKARVKEY
ARNKNIHYYFMALKNDEIIDATQKGNCSRFMNHSCEPNCETQKWTVNGQLRVGFFTTKLV
PSGSELTFDYQFQRYGKEAQKCFCGSANCRGYLGGENRVSIRAAGGKMKKERSRK
Sequence of entity 2 (B), FASTA
>8Q5P_2 Activated CDC42 kinase 1 (chains B)
QHLGGVMKPTYD

Ligands and cofactors

IDNameFormulaCopies
SAMS-adenosylmethionineC15 H22 N6 O5 S1
ZNZinc ionZn3

Primary citation

Structural and enzymatic evidence for the methylation of the ACK1 tyrosine kinase by the histone lysine methyltransferase SETD2. Le Coadou, L., Berthelet, J., Mechaly, A.E. et al. Biochem Biophys Res Commun (2024) 695:149400-149400. DOI 10.1016/j.bbrc.2023.149400 · PubMed

Other PDB entries of the same protein (UniProt Q9BYW2 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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