Crystal Structure of the MRG15 MRG domain. Determined by X-ray diffraction at 2.3 Å resolution. Released 28 Feb 2006.
Explore 2AQL in 3D Show helices and sheets RCSB PDB PDBe
2AQL contains 28 α-helices and 8 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 | 159-161 | 3 | |
| α-helix | 162-164 | 3 | |
| α-helix | 165-176 | 12 | |
| β-strand | 180-182 | 3 | 1 |
| β-strand | 189 | 1 | 2 |
| α-helix | 190-200 | 11 | |
| α-helix | 212-228 | 17 | |
| α-helix | 236-238 | 3 | |
| α-helix | 239-248 | 10 | |
| α-helix | 254-256 | 3 | |
| β-strand | 259 | 1 | 2 |
| α-helix | 260-274 | 15 | |
| α-helix | 281-300 | 20 | |
| α-helix | 302-305 | 4 | |
| α-helix | 308-310 | 3 | |
| β-strand | 311-313 | 3 | 1 |
| α-helix | 314-315 | 2 | |
| α-helix | 316-319 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 159-161 | 3 | |
| α-helix | 162-164 | 3 | |
| α-helix | 165-176 | 12 | |
| β-strand | 180-182 | 3 | 3 |
| β-strand | 189 | 1 | 4 |
| α-helix | 190-200 | 11 | |
| α-helix | 214-228 | 15 | |
| α-helix | 236-238 | 3 | |
| α-helix | 239-248 | 10 | |
| α-helix | 254-256 | 3 | |
| β-strand | 259 | 1 | 4 |
| α-helix | 260-268 | 9 | |
| α-helix | 277-280 | 4 | |
| α-helix | 281-300 | 20 | |
| α-helix | 302-305 | 4 | |
| α-helix | 308-310 | 3 | |
| β-strand | 311-313 | 3 | 3 |
| α-helix | 314-315 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mortality factor 4-like protein 1 | A, B | protein | 173 | Homo sapiens | Q9UBU8 (AlphaFold model) |
>2AQL_1 Mortality factor 4-like protein 1 (chains A, B) MNRVEVKVKIPEELKPWLVDDWDLITRQKQLFYLPAKKNVDSILEDYANYKKSRGNTDNK EYAVNEVVAGIKEYFNVMLGTQLLYKFERPQYAEILADHPDAPMSQVYGAPHLLRLFVRI GAMLAYTPLDEKSLALLLNYLHDFLKYLAKNSATLFSASDYEVAPPEYHRKAV
Multipurpose MRG domain involved in cell senescence and proliferation exhibits structural homology to a DNA-interacting domain. Bowman, B.R., Moure, C.M., Kirtane, B.M. et al. Structure (2006) 14:151-158. DOI 10.1016/j.str.2005.08.019 · PubMed
Other PDB entries of the same protein (UniProt Q9UBU8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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