Sir2 homologue S24A mutant-ADP ribose complex. Determined by X-ray diffraction at 1.8 Å resolution. Released 8 Apr 2003.
Explore 1M2H in 3D Show helices and sheets RCSB PDB PDBe
1M2H contains 19 α-helices and 11 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 | 3-10 | 8 | |
| β-strand | 15-19 | 5 | 1 |
| α-helix | 21-23 | 3 | |
| α-helix | 25-27 | 3 | |
| α-helix | 38-41 | 4 | |
| α-helix | 44-47 | 4 | |
| α-helix | 50-55 | 6 | |
| α-helix | 57-73 | 17 | |
| α-helix | 78-88 | 11 | |
| β-strand | 92-97 | 6 | 1 |
| α-helix | 103-107 | 5 | |
| β-strand | 112-114 | 3 | 1 |
| β-strand | 117-124 | 8 | 2 |
| β-strand | 130-132 | 3 | 2 |
| α-helix | 136-138 | 3 | |
| α-helix | 142-143 | 2 | |
| β-strand | 144 | 1 | 3 |
| α-helix | 150 | 1 | |
| β-strand | 151 | 1 | 3 |
| β-strand | 152-156 | 5 | 2 |
| α-helix | 157-158 | 2 | |
| α-helix | 162-164 | 3 | |
| α-helix | 165-177 | 13 | |
| β-strand | 180-184 | 5 | 1 |
| α-helix | 193-195 | 3 | |
| α-helix | 196-202 | 7 | |
| β-strand | 206-210 | 5 | 1 |
| α-helix | 218-220 | 3 | |
| β-strand | 223-225 | 3 | 1 |
| α-helix | 229-245 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Silent Information Regulator 2 | A | protein | 249 | Archaeoglobus fulgidus | O28597 (AlphaFold model) |
>1M2H_1 Silent Information Regulator 2 (chains A) MDEKLLKTIAESKYLVALTGAGVAAESGIPTFRGKDGLWNRYRPEELANPQAFAKDPEKV WKWYAWRMEKVFNAQPNKAHQAFAELERLGVLKCLITQNVDDLHERAGSRNVIHLHGSLR VVRCTSCNNSFEVESAPKIPPLPKCDKCGSLLRPGVVWFGEMLPPDVLDRAMREVERADV IIVAGTSAVVQPAASLPLIVKQRGGAIIEINPDETPLTPIADYSLRGKAGEVMDELVRHV RKALSLKLN
Structural basis for the NAD-dependent deacetylase mechanism of Sir2. Chang, J.H., Kim, H.C., Hwang, K.Y. et al. J Biol Chem (2002) 277:34489-34498. DOI 10.1074/jbc.M205460200 · PubMed
Other PDB entries of the same protein (UniProt O28597 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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