5QT1: Histone-lysine N-methyltransferase SETDB1

PanDDA analysis group deposition -- Partial occupancy interpretation of PanDDA event map: SETDB1 in complex with FMOMB000017a. Determined by X-ray diffraction at 1.58 Å resolution. Released 21 Aug 2019.

Method
X-ray diffraction
Resolution
1.58 Å
Organism
Homo sapiens
Chains
1
Atoms
1,980
Mol. weight
26.9 kDa
Ligands
DSJ
Released
21 Aug 2019

Explore 5QT1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5QT1 contains 6 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.

Chain A: 6 helices, 19 β-strands

ElementResiduesLengthSheet
β-strand191-19221
β-strand194-19522
β-strand198-19922
β-strand203-20751
β-strand213-224121
β-strand227-23481
β-strand239-24241
α-helix244-2463
β-strand247-24821
α-helix252-2543
α-helix255-2573
β-strand263-27083
β-strand273-283113
β-strand293-29753
β-strand302-30543
α-helix307-3093
β-strand310-31233
β-strand31311
α-helix320-3234
α-helix327-33913
β-strand353-35864
β-strand361-371114
β-strand374-37964
β-strand384-38964
β-strand39514

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone-lysine N-methyltransferase SETDB1Aprotein225Homo sapiensQ15047 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5QT1_1 Histone-lysine N-methyltransferase SETDB1 (chains A)
MHHHHHHSSGRENLYFQGDLIVSMRILGKKRTKTWHKGTLIAIQTVGPGKKYKVKFDNKG
KSLLSGNHIAYDYHPPADKLYVGSRVVAKYKDGNQVWLYAGIVAETPNVKNKLRFLIFFD
DGYASYVTQSELYPICRPLKKTWEDIEDISCRDFIEEYVTAYPNRPMVLLKSGQLIKTEW
EGTWWKSRVEEVDGSLVRILFLDDKRCEWIYRGSTRLEPMFSMKT

Ligands and cofactors

IDNameFormulaCopies
DSJ1-(4-amino-2-hydroxyphenyl)ethan-1-oneC8 H9 N O21

Water and common crystallization additives (DMS, EDO, UNX, SO4) are not listed.

Primary citation

PanDDA analysis group deposition. Harding, R.J., Tempel, W., DOUANGAMATH, A. et al. To be published.

Other PDB entries of the same protein (UniProt Q15047 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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