Mms2/Ubc13~Ubiquitin. Determined by X-ray diffraction at 2.5 Å resolution. Released 19 Sept 2006.
Explore 2GMI in 3D Show helices and sheets RCSB PDB PDBe
2GMI contains 16 α-helices and 25 β-strands across 3 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 | 6-17 | 12 | |
| α-helix | 19-20 | 2 | |
| β-strand | 23-28 | 6 | 1 |
| β-strand | 31-40 | 10 | 1 |
| β-strand | 50-57 | 8 | 1 |
| α-helix | 66-67 | 2 | |
| β-strand | 68-71 | 4 | 1 |
| β-strand | 77 | 1 | 2 |
| β-strand | 80 | 1 | 2 |
| β-strand | 85 | 1 | 1 |
| β-strand | 86 | 1 | 2 |
| α-helix | 89-91 | 3 | |
| α-helix | 101-113 | 13 | |
| α-helix | 123-131 | 9 | |
| α-helix | 133-147 | 15 | |
| β-strand | 149-150 | 2 | 1 |
| α-helix | 151 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-18 | 13 | |
| β-strand | 26-30 | 5 | 3 |
| β-strand | 40-46 | 7 | 3 |
| α-helix | 47-48 | 2 | |
| β-strand | 57-63 | 7 | 3 |
| β-strand | 74-77 | 4 | 3 |
| β-strand | 79 | 1 | 4 |
| β-strand | 86 | 1 | 5 |
| β-strand | 92 | 1 | 3 |
| β-strand | 93 | 1 | 5 |
| α-helix | 94 | 1 | |
| α-helix | 109-118 | 10 | |
| β-strand | 136 | 1 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 502-507 | 6 | 6 |
| β-strand | 512-516 | 5 | 6 |
| β-strand | 522 | 1 | 7 |
| α-helix | 523-534 | 12 | |
| α-helix | 538-540 | 3 | |
| β-strand | 542-545 | 4 | 6 |
| β-strand | 548-549 | 2 | 6 |
| β-strand | 555 | 1 | 7 |
| α-helix | 557-559 | 3 | |
| β-strand | 566-570 | 5 | 6 |
| α-helix | 572-574 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-conjugating enzyme E2 13 | A | protein | 152 | Saccharomyces cerevisiae | P52490 (AlphaFold model) |
| Ubiquitin-conjugating enzyme variant MMS2 | B | protein | 137 | Saccharomyces cerevisiae | P53152 (AlphaFold model) |
| Ubiquitin | C | protein | 76 | Homo sapiens | P0CG48 (AlphaFold model) |
>2GMI_1 Ubiquitin-conjugating enzyme E2 13 (chains A) MASLPKRIIKETEKLVSDPVPGITAEPHDDNLRYFQVTIEGPEQSPYEDGIFELELYLPD DYPMEAPKVRFLTKIYHPNIDRLGRISLDVLKTNWSPALQIRTVLLSIQALLASPNPNDP LANDVAEDWIKNEQGAKAKAREWTKLYAKKKP
>2GMI_2 Ubiquitin-conjugating enzyme variant MMS2 (chains B) MSKVPRNFRLLEELEKGEKGFGPESCSYGLADSDDITMTKWNGTILGPPHSNHENRIYSL SIDCGPNYPDSPPKVTFISKINLPCVNPTTGEVQTDFHTLRDWKRAYTMETLLLDLRKEM ATPANKKLRQPKEGETF
>2GMI_3 Ubiquitin (chains C) MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG
Mms2-Ubc13 covalently bound to ubiquitin reveals the structural basis of linkage-specific polyubiquitin chain formation. Eddins, M.J., Carlile, C.M., Gomez, K.M. et al. Nat Struct Mol Biol (2006) 13:915-920. DOI 10.1038/nsmb1148 · PubMed
Other PDB entries of the same protein (UniProt P52490 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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