6VFO: PHD of mouse UHRF1

Solution structure of the PHD of mouse UHRF1 (NP95). Determined by solution NMR. Released 17 Jun 2020.

Method
Solution NMR
Organism
Mus musculus
Chains
1
Atoms
600
Mol. weight
8.89 kDa
Ligands
ZN
Released
17 Jun 2020

Explore 6VFO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6VFO contains 5 α-helices and 4 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: 5 helices, 4 β-strands

ElementResiduesLengthSheet
α-helix319-3213
β-strand32311
β-strand32811
α-helix332-3343
β-strand335-33842
β-strand343-34642
α-helix347-3493
α-helix353-3542
α-helix366-3683

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligase UHRF1Aprotein78Mus musculusQ8VDF2 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6VFO_1 E3 ubiquitin-protein ligase UHRF1 (chains A)
SGPSCRFCKDDENKPCRKCACHVCGGREAPEKQLLCDECDMAFHLYCLKPPLTSVPPEPE
WYCPSCRTDSSEVVQAGE

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn3

Primary citation

Alternative splicing and allosteric regulation modulate the chromatin binding of UHRF1. Tauber, M., Kreuz, S., Lemak, A. et al. Nucleic Acids Res (2020) 48:7728-7747. DOI 10.1093/nar/gkaa520 · PubMed

Other PDB entries of the same protein (UniProt Q8VDF2 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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