Solution structure of the MRG15-MRGBP complex. Determined by solution NMR. Released 27 May 2015.
Explore 2N1D in 3D Show helices and sheets RCSB PDB PDBe
2N1D contains 17 α-helices and 4 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 | 73-75 | 3 | |
| α-helix | 77-83 | 7 | |
| α-helix | 88-93 | 6 | |
| β-strand | 104 | 1 | 1 |
| α-helix | 109-115 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 165-172 | 8 | |
| α-helix | 173-177 | 5 | |
| β-strand | 180-181 | 2 | 2 |
| α-helix | 190-204 | 15 | |
| α-helix | 209-226 | 18 | |
| β-strand | 234 | 1 | 1 |
| α-helix | 236-238 | 3 | |
| α-helix | 239-248 | 10 | |
| α-helix | 254-257 | 4 | |
| α-helix | 264-273 | 10 | |
| α-helix | 281-300 | 20 | |
| α-helix | 302-304 | 3 | |
| α-helix | 308-310 | 3 | |
| β-strand | 312-313 | 2 | 2 |
| α-helix | 314-315 | 2 | |
| α-helix | 316-319 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| MRG/MORF4L-binding protein | A | protein | 54 | Homo sapiens | Q9NV56 (AlphaFold model) |
| Mortality factor 4-like protein 1 | B | protein | 172 | Homo sapiens | Q9UBU8 (AlphaFold model) |
>2N1D_1 MRG/MORF4L-binding protein (chains A) SNAGRQVPSKVIWDHLSTMYDMQALHESEILPFPNPERNFVLPEEIIQEVREGK
>2N1D_2 Mortality factor 4-like protein 1 (chains B) SNAEVKVKIPEELKPWLVDDWDLITRQKQLFYLPAKKNVDSILEDYANYKKSRGNTDNKE YAVNEVVAGIKEYFNVMLGTQLLYKFERPQYAEILADHPDAPMSQVYGAPHLLRLFVRIG AMLAYTPLDEKSLALLLNYLHDFLKYLAKNSATLFSASDYEVAPPEYHRKAV
Structural Basis for Multi-specificity of MRG Domains. Xie, T., Zmyslowski, A.M., Zhang, Y. et al. Structure (2015) 23:1049-1057. DOI 10.1016/j.str.2015.03.020 · PubMed
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