Crystal structure of MRG domain from human MRG15. Determined by X-ray diffraction at 2.2 Å resolution. Released 14 Nov 2006.
Explore 2F5J in 3D Show helices and sheets RCSB PDB PDBe
2F5J contains 31 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 | 158-161 | 4 | |
| α-helix | 162-164 | 3 | |
| α-helix | 165-176 | 12 | |
| β-strand | 180-182 | 3 | 1 |
| β-strand | 189 | 1 | 2 |
| α-helix | 190-202 | 13 | |
| α-helix | 213-232 | 20 | |
| α-helix | 236-238 | 3 | |
| α-helix | 239-248 | 10 | |
| α-helix | 254-257 | 4 | |
| 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 | 158-161 | 4 | |
| α-helix | 162-164 | 3 | |
| α-helix | 165-172 | 8 | |
| α-helix | 173-177 | 5 | |
| β-strand | 180-182 | 3 | 3 |
| β-strand | 189 | 1 | 4 |
| α-helix | 190-201 | 12 | |
| α-helix | 214-232 | 19 | |
| α-helix | 236-238 | 3 | |
| α-helix | 239-248 | 10 | |
| α-helix | 254-257 | 4 | |
| β-strand | 259 | 1 | 4 |
| α-helix | 260-269 | 10 | |
| α-helix | 270-272 | 3 | |
| α-helix | 277-279 | 3 | |
| 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 | |
| α-helix | 316-320 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mortality factor 4-like protein 1 | A, B | protein | 181 | Homo sapiens | Q9UBU8 (AlphaFold model) |
>2F5J_1 Mortality factor 4-like protein 1 (chains A, B) MNRVEVKVKIPEELKPWLVDDWDLITRQKQLFYLPAKKNVDSILEDYANYKKSRGNTDNK EYAVNEVVAGIKEYFNVMLGTQLLYKFERPQYAEILADHPDAPMSQVYGAPHLLRLFVRI GAMLAYTPLDEKSLALLLNYLHDFLKYLAKNSATLFSASDYEVAPPEYHRKAVLEHHHHH H
The MRG domain of human MRG15 uses a shallow hydrophobic pocket to interact with the N-terminal region of PAM14. Zhang, P., Zhao, J., Wang, B. et al. Protein Sci (2006) 15:2423-2434. DOI 10.1110/ps.062397806 · 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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