4RT4: Dpy30

Crystal structure of Dpy30 complexed with Bre2. Determined by X-ray diffraction at 2.0 Å resolution. Released 7 Oct 2015.

Method
X-ray diffraction
Resolution
2.0 Å
Organisms
Homo sapiens, Saccharomyces cerevisiae S288c
Chains
5
Atoms
2,097
Mol. weight
33.89 kDa
Released
7 Oct 2015

Explore 4RT4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4RT4 contains 19 α-helices and 0 β-strands across 5 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.

Chains A and B: 5 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix48-503
α-helix53-586
α-helix62-7514
α-helix80-9112
α-helix92-943
Chains C and D: 4 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix48-503
α-helix53-608
α-helix62-7514
α-helix80-9516
Chain E: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix482-49918

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein dpy-30 homologA, B, C, Dprotein66Homo sapiensQ9C005 (AlphaFold model)
Peptide from COMPASS component BRE2Eprotein30Saccharomyces cerevisiae S288cP43132 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>4RT4_1 Protein dpy-30 homolog (chains A, B, C, D)
SSKQKVDLQSLPTRAYLDQTVVPILLQGLAVLAKERPPNPIEFLASYLLKNKAQFEDRNL
ERPHRD
Sequence of entity 2 (E), FASTA
>4RT4_2 Peptide from COMPASS component BRE2 (chains E)
NTLDTLYKEQIAEDIVWDIIDELEQIALQQ

Primary citation

Structural implications of Dpy30 oligomerization for MLL/SET1 COMPASS H3K4 trimethylation. Zhang, H., Li, M., Gao, Y. et al. Protein Cell (2015) 6:147-151. DOI 10.1007/s13238-014-0127-z · PubMed

Other PDB entries of the same protein (UniProt Q9C005 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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