Structure of mouse ORC1 BAH domain bound to H4K20me2. Determined by X-ray diffraction at 1.95 Å resolution. Released 7 Mar 2012.
Explore 4DOW in 3D Show helices and sheets RCSB PDB PDBe
4DOW contains 19 α-helices and 31 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 |
|---|---|---|---|
| β-strand | 14-16 | 3 | 1 |
| α-helix | 20-21 | 2 | |
| α-helix | 23 | 1 | |
| β-strand | 28-31 | 4 | 2 |
| β-strand | 33-37 | 5 | 1 |
| β-strand | 43-47 | 5 | 1 |
| β-strand | 48 | 1 | 3 |
| β-strand | 50 | 1 | 3 |
| β-strand | 51-54 | 4 | 2 |
| α-helix | 61-62 | 2 | |
| β-strand | 63-73 | 11 | 2 |
| β-strand | 80-89 | 10 | 2 |
| α-helix | 91-93 | 3 | |
| α-helix | 96-99 | 4 | |
| α-helix | 100-102 | 3 | |
| β-strand | 110-114 | 5 | 2 |
| β-strand | 122-124 | 3 | 2 |
| α-helix | 125-127 | 3 | |
| β-strand | 128-132 | 5 | 2 |
| β-strand | 134-136 | 3 | 2 |
| α-helix | 141-144 | 4 | |
| β-strand | 153-159 | 7 | 2 |
| β-strand | 164-166 | 3 | 2 |
| α-helix | 167-168 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 14-16 | 3 | 4 |
| α-helix | 20-21 | 2 | |
| α-helix | 23 | 1 | |
| β-strand | 28-30 | 3 | 5 |
| β-strand | 33-37 | 5 | 4 |
| β-strand | 43-47 | 5 | 4 |
| β-strand | 51-54 | 4 | 5 |
| α-helix | 61-62 | 2 | |
| β-strand | 63-73 | 11 | 5 |
| β-strand | 80-87 | 8 | 5 |
| β-strand | 88-89 | 2 | 6 |
| α-helix | 91-93 | 3 | |
| α-helix | 96-99 | 4 | |
| α-helix | 100-102 | 3 | |
| β-strand | 110-114 | 5 | 6 |
| β-strand | 119 | 1 | 7 |
| β-strand | 122-124 | 3 | 5 |
| α-helix | 125-127 | 3 | |
| β-strand | 128-132 | 5 | 5 |
| β-strand | 134-136 | 3 | 6 |
| β-strand | 153-159 | 7 | 6 |
| β-strand | 164-166 | 3 | 6 |
| α-helix | 167-168 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 15-18 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 15-20 | 6 | |
| β-strand | 22 | 1 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Origin recognition complex subunit 1 | A, B | protein | 163 | Mus musculus | Q9Z1N2 (AlphaFold model) |
| Histone H4 | C, D | protein | 12 | Mus musculus | P62806 (AlphaFold model) |
>4DOW_1 Origin recognition complex subunit 1 (chains A, B) SKTRQTFSWVGRPLPNRKQFQQMYREICMKINDGSEIHIKVGQFVLIQGEDNKKPYVAKL IELFQNGAEVPPKKCARVQWFVRFLEIPVSKRHLLGRSPPAQEIFWYDCSDWDNKINVET IIGPVQVVALAPEEVIPVDQKSEETLFVKLSWNKKDFAPLPPE
>4DOW_2 Histone H4 (chains C, D) GAKRHRKVLRDN
The BAH domain of ORC1 links H4K20me2 to DNA replication licensing and Meier-Gorlin syndrome. Kuo, A.J., Song, J., Cheung, P. et al. Nature (2012) 484:115-119. DOI 10.1038/nature10956 · PubMed
Other PDB entries of the same protein (UniProt Q9Z1N2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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