4RTA: Protein dpy-30 homolog

Cystal structure of the Dpy30 for MLL/SET1 COMPASS H3K4 trimethylation. Determined by X-ray diffraction at 2.12 Å resolution. Released 7 Oct 2015.

Method
X-ray diffraction
Resolution
2.12 Å
Organism
Homo sapiens
Chains
2
Atoms
1,162
Mol. weight
24.48 kDa
Released
7 Oct 2015

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

Secondary structure: helices and β-sheets

4RTA contains 8 α-helices and 0 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: 3 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix53-608
α-helix62-7514
α-helix80-9516
Chain B: 5 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix31-344
α-helix48-503
α-helix53-608
α-helix62-7514
α-helix80-9516

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein dpy-30 homologA, Bprotein106Homo sapiensQ9C005 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4RTA_1 Protein dpy-30 homolog (chains A, B)
MEPEQMLEGQTQVAENPHSEYGLTDNVERIVENEKINAEKSSKQKVDLQSLPTRAYLDQT
VVPILLQGLAVLAKERPPNPIEFLASYLLKNKAQFEDRNLERPHRD

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:

Browse structure collections

About this viewer

MolViewer shows 4RTA 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.