Crystal Structure of APO Human SETD8. Determined by X-ray diffraction at 2.0 Å resolution. Released 7 Mar 2018.
Explore 5V2N in 3D Show helices and sheets RCSB PDB PDBe
5V2N contains 8 α-helices and 13 β-strands across 1 chain. 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 | 192-194 | 3 | |
| α-helix | 195-212 | 18 | |
| β-strand | 218-223 | 6 | 1 |
| β-strand | 227-232 | 6 | 1 |
| β-strand | 236 | 1 | 2 |
| β-strand | 241-244 | 4 | 3 |
| β-strand | 248-252 | 5 | 4 |
| α-helix | 255-262 | 8 | |
| β-strand | 273-277 | 5 | 4 |
| β-strand | 280-285 | 6 | 4 |
| α-helix | 294-296 | 3 | |
| α-helix | 297 | 1 | |
| β-strand | 298-299 | 2 | 5 |
| β-strand | 305-312 | 8 | 3 |
| β-strand | 315-322 | 8 | 3 |
| β-strand | 326 | 1 | 2 |
| α-helix | 330 | 1 | |
| β-strand | 331 | 1 | 1 |
| α-helix | 332 | 1 | |
| β-strand | 333-334 | 2 | 5 |
| α-helix | 340-345 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| N-lysine methyltransferase KMT5A | A | protein | 165 | Homo sapiens | Q9NQR1 (AlphaFold model) |
>5V2N_1 N-lysine methyltransferase KMT5A (chains A) GGSSRKSKAELQSEERKRIDELIESGKEEGMKIDLIDGKGRGVIATKQFSRGDFVVEYHG DLIEITDAAARAALYAQDPSTGCYMYYFQYLSKTYCVDATRETNRLGRLINHSKCGNCQT KLHDIDGVPHLILIASRDIAAGEELLYDYGDRSKASIEAHPWLKH
The dynamic conformational landscape of the protein methyltransferase SETD8. Chen, S., Wiewiora, R.P., Meng, F. et al. Elife (2019) 8. DOI 10.7554/eLife.45403 · PubMed
Other PDB entries of the same protein (UniProt Q9NQR1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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