Mouse HP1 (M31) C terminal (shadow chromo) domain. Determined by solution NMR. Released 9 Apr 2000.
Explore 1DZ1 in 3D Show helices and sheets RCSB PDB PDBe
1DZ1 contains 8 α-helices and 12 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 112-115 | 4 | |
| α-helix | 117-118 | 2 | |
| β-strand | 119 | 1 | 1 |
| β-strand | 125-127 | 3 | 2 |
| β-strand | 132-134 | 3 | 2 |
| β-strand | 138 | 1 | 1 |
| β-strand | 141 | 1 | 1 |
| β-strand | 147-148 | 2 | 2 |
| α-helix | 149-155 | 7 | |
| α-helix | 157-166 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Modifier 1 protein | A, B | protein | 70 | MUS MUSCULUS | P83917 (AlphaFold model) |
>1DZ1_1 MODIFIER 1 PROTEIN (chains A, B) HMKEESEKPRGFARGLEPERIIGATDSSGELMFLMKWKNSDEADLVPAKEANVKCPQVVI SFYEERLTWH
The Structure of Mouse Hp1 Suggests a Unique Mode of Single Peptide Recognition by the Shadow Chromo Domain Dimer. Brasher, S.V., Smith, B.O., Fogh, R.H. et al. EMBO J (2000) 19:1587. DOI 10.1093/EMBOJ/19.7.1587 · PubMed
Other PDB entries of the same protein (UniProt P83917 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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