Crystal structure of TFB1M and h45 with SAM in homo sapiens. Determined by X-ray diffraction at 2.99 Å resolution. Released 5 Jun 2019.
Explore 6AAX in 3D Show helices and sheets RCSB PDB PDBe
6AAX contains 39 α-helices and 20 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 |
|---|---|---|---|
| β-strand | 37 | 1 | 1 |
| α-helix | 41-50 | 10 | |
| β-strand | 58-62 | 5 | 2 |
| α-helix | 68-74 | 7 | |
| β-strand | 80-85 | 6 | 2 |
| α-helix | 88-90 | 3 | |
| α-helix | 91-99 | 9 | |
| β-strand | 105-109 | 5 | 2 |
| α-helix | 117-119 | 3 | |
| α-helix | 123-125 | 3 | |
| α-helix | 132-134 | 3 | |
| β-strand | 136-140 | 5 | 2 |
| α-helix | 144-159 | 16 | |
| α-helix | 163-167 | 5 | |
| β-strand | 171-177 | 7 | 2 |
| α-helix | 178-185 | 8 | |
| α-helix | 195-201 | 7 | |
| β-strand | 204-212 | 9 | 2 |
| α-helix | 214-216 | 3 | |
| β-strand | 218 | 1 | 1 |
| α-helix | 220-221 | 2 | |
| β-strand | 225-232 | 8 | 2 |
| α-helix | 242-252 | 11 | |
| α-helix | 261-264 | 4 | |
| α-helix | 265-267 | 3 | |
| α-helix | 270-284 | 15 | |
| α-helix | 292-294 | 3 | |
| α-helix | 297-312 | 16 | |
| α-helix | 315-317 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 37 | 1 | 3 |
| α-helix | 41-49 | 9 | |
| β-strand | 58-62 | 5 | 4 |
| α-helix | 68-72 | 5 | |
| β-strand | 80-85 | 6 | 4 |
| α-helix | 88-90 | 3 | |
| α-helix | 91-99 | 9 | |
| β-strand | 106-109 | 4 | 4 |
| α-helix | 123-125 | 3 | |
| β-strand | 127 | 1 | 5 |
| α-helix | 132-134 | 3 | |
| β-strand | 136-140 | 5 | 4 |
| α-helix | 144-160 | 17 | |
| α-helix | 163-165 | 3 | |
| β-strand | 168 | 1 | 5 |
| β-strand | 171-177 | 7 | 4 |
| α-helix | 178-185 | 8 | |
| α-helix | 195-201 | 7 | |
| β-strand | 204-212 | 9 | 4 |
| α-helix | 214-216 | 3 | |
| β-strand | 218 | 1 | 3 |
| α-helix | 220-221 | 2 | |
| β-strand | 225-232 | 8 | 4 |
| α-helix | 242-252 | 11 | |
| α-helix | 260-264 | 5 | |
| α-helix | 265-267 | 3 | |
| α-helix | 270-273 | 4 | |
| α-helix | 276-282 | 7 | |
| α-helix | 292-294 | 3 | |
| α-helix | 297-312 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Dimethyladenosine transferase 1, mitochondrial | A, C | protein | 319 | Homo sapiens | Q8WVM0 (AlphaFold model) |
| RNA (28-mer) | B, D | RNA | 28 | Homo sapiens |
>6AAX_1 Dimethyladenosine transferase 1, mitochondrial (chains A, C) QAAKQLSQNFLLDLRLTDKIVRKAGNLTNAYVYEVGPGPGGITRSILNADVAELLVVEKD TRFIPGLQMLSDAAPGKLRIVHGDVLTFKVEKAFSESLKRPWEDDPPNVHIIGNLPFSVS TPLIIKWLENISCRDGPFVYGRTQMTLTFQKEVAERLAANTGSKQRSRLSVMAQYLCNVR HIFTIPGQAFVPKPEVDVGVVHFTPLIQPKIEQPFKLVEKVVQNVFQFRRKYCHRGLRML FPEAQRLESTGRLLELADIDPTLRPRQLSISHFKSLCDVYRKMCDEDPQLFAYNFREELK RRKSKNEEKEEDDAENYRL
>6AAX_2 RNA (28-mer) (chains B, D) GGUAAGUGUACUGGAAAGUGCACUUGCC
| ID | Name | Formula | Copies |
|---|---|---|---|
| SAM | S-adenosylmethionine | C15 H22 N6 O5 S | 2 |
Water and common crystallization additives (PEG) are not listed.
Structural insights into dimethylation of 12S rRNA by TFB1M: indispensable role in translation of mitochondrial genes and mitochondrial function. Liu, X., Shen, S., Wu, P. et al. Nucleic Acids Res (2019) 47:7648-7665. DOI 10.1093/nar/gkz505 · PubMed
Other PDB entries of the same protein (UniProt Q8WVM0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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