Crystal structure of a methyltransferase. Determined by X-ray diffraction at 1.2 Å resolution. Released 25 Jul 2018.
Explore 6DUB in 3D Show helices and sheets RCSB PDB PDBe
6DUB contains 29 α-helices and 25 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 | 64-76 | 13 | |
| α-helix | 83-86 | 4 | |
| α-helix | 91-93 | 3 | |
| α-helix | 94-105 | 12 | |
| β-strand | 109 | 1 | 1 |
| β-strand | 115 | 1 | 1 |
| β-strand | 119-123 | 5 | 2 |
| α-helix | 129-130 | 2 | |
| α-helix | 131-135 | 5 | |
| β-strand | 141-146 | 6 | 2 |
| α-helix | 149-158 | 10 | |
| α-helix | 160-165 | 6 | |
| β-strand | 166-171 | 6 | 2 |
| α-helix | 174-176 | 3 | |
| α-helix | 179-180 | 2 | |
| β-strand | 184-190 | 7 | 2 |
| α-helix | 193-195 | 3 | |
| α-helix | 198-210 | 13 | |
| β-strand | 212-223 | 12 | 2 |
| β-strand | 224-225 | 2 | 3 |
| β-strand | 229-232 | 4 | 3 |
| β-strand | 237-241 | 5 | 3 |
| α-helix | 242-251 | 10 | |
| β-strand | 256-261 | 6 | 2 |
| α-helix | 262-263 | 2 | |
| α-helix | 270-271 | 2 | |
| β-strand | 272-277 | 6 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 64-76 | 13 | |
| α-helix | 83-86 | 4 | |
| α-helix | 91-93 | 3 | |
| α-helix | 94-108 | 15 | |
| β-strand | 109 | 1 | 4 |
| β-strand | 115 | 1 | 4 |
| β-strand | 119-123 | 5 | 5 |
| α-helix | 129-130 | 2 | |
| α-helix | 131-135 | 5 | |
| β-strand | 141-146 | 6 | 5 |
| α-helix | 149-158 | 10 | |
| α-helix | 160-165 | 6 | |
| β-strand | 166-171 | 6 | 5 |
| α-helix | 174-176 | 3 | |
| β-strand | 184-190 | 7 | 5 |
| α-helix | 193-195 | 3 | |
| α-helix | 198-210 | 13 | |
| β-strand | 212-223 | 12 | 5 |
| β-strand | 225 | 1 | 6 |
| β-strand | 230-232 | 3 | 7 |
| β-strand | 237-239 | 3 | 7 |
| β-strand | 241 | 1 | 6 |
| α-helix | 242-251 | 10 | |
| β-strand | 256-261 | 6 | 5 |
| α-helix | 262-263 | 2 | |
| α-helix | 270-271 | 2 | |
| β-strand | 272-277 | 6 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alpha N-terminal protein methyltransferase 1B | A, B | protein | 222 | Homo sapiens | Q5VVY1 (AlphaFold model) |
| RCC1 | E, F | protein | 6 | Homo sapiens | P18754 (AlphaFold model) |
>6DUB_1 Alpha N-terminal protein methyltransferase 1B (chains A, B) GTSQVINGEMQFYARAKLFYQEVPATEEGMMGNFIELSSPDIQASQKFLRKFVGGPGRAG TDCALDCGSGIGRVSKHVLLPVFNSVELVDMMESFLLEAQNYLQVKGDKVESYHCYSLQE FTPPFRRYDVIWIQWVSGHLTDKDLLAFLSRCRDGLKENGIIILKDNVAREGCILDLSDS SVTRDMDILRSLIRKSGLVVLGQEKQDGFPEQCIPVWMFALH
>6DUB_2 RCC1 (chains E, F) XPKRIA
| ID | Name | Formula | Copies |
|---|---|---|---|
| SAH | S-adenosyl-L-homocysteine | C14 H20 N6 O5 S | 2 |
Water and common crystallization additives (GOL, UNX) are not listed.
An asparagine/glycine switch governs product specificity of human N-terminal methyltransferase NTMT2. Dong, C., Dong, G., Li, L. et al. Commun Biol (2018) 1:183-183. DOI 10.1038/s42003-018-0196-2 · PubMed
Other PDB entries of the same protein (UniProt Q5VVY1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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