Crystal structure of HP1alpha chromoshadow domain. Determined by X-ray diffraction at 2.15 Å resolution. Released 11 Jun 2025.
Explore 9CEA in 3D Show helices and sheets RCSB PDB PDBe
9CEA contains 16 α-helices and 12 β-strands across 4 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 | 116-119 | 4 | |
| α-helix | 121-122 | 2 | |
| β-strand | 123-130 | 8 | 1 |
| β-strand | 137-142 | 6 | 1 |
| β-strand | 149-152 | 4 | 1 |
| α-helix | 153-159 | 7 | |
| α-helix | 161-171 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 116-119 | 4 | |
| α-helix | 121-122 | 2 | |
| β-strand | 123-130 | 8 | 2 |
| β-strand | 137-142 | 6 | 2 |
| β-strand | 149-152 | 4 | 2 |
| α-helix | 153-159 | 7 | |
| α-helix | 161-172 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 116-119 | 4 | |
| α-helix | 121-122 | 2 | |
| β-strand | 123-132 | 10 | 3 |
| β-strand | 135-142 | 8 | 3 |
| β-strand | 149-152 | 4 | 3 |
| α-helix | 153-159 | 7 | |
| α-helix | 161-171 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 116-119 | 4 | |
| α-helix | 121-122 | 2 | |
| β-strand | 123-132 | 10 | 4 |
| β-strand | 135-142 | 8 | 4 |
| β-strand | 149-152 | 4 | 4 |
| α-helix | 153-159 | 7 | |
| α-helix | 161-170 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Chromobox protein homolog 5 | A, B, C, D | protein | 63 | Homo sapiens | P45973 (AlphaFold model) |
>9CEA_1 Chromobox protein homolog 5 (chains A, B, C, D) IARGFERGLEPEKIIGATDSCGDLMFLMKWKDTDEADLVLAKEANVKCPQIVIAFYEERL TWH
The HP1 box of KAP1 organizes HP1 alpha for silencing of endogenous retroviral elements in embryonic stem cells. Gaurav, N., O'Hara, R., Hyder, U. et al. Nat Commun (2025) 16:5066-5066. DOI 10.1038/s41467-025-60279-2 · PubMed
Other PDB entries of the same protein (UniProt P45973 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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