Complex structure of MyUb (1080-1122) of human Myosin VI with K63-diUb. Determined by solution NMR. Released 9 Mar 2016.
Explore 2N13 in 3D Show helices and sheets RCSB PDB PDBe
2N13 contains 11 α-helices and 14 β-strands across 4 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 | 20-29 | 10 | |
| α-helix | 33-48 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 102-106 | 5 | 1 |
| β-strand | 112-116 | 5 | 1 |
| β-strand | 122 | 1 | 2 |
| α-helix | 123-133 | 11 | |
| α-helix | 138-140 | 3 | |
| β-strand | 143-145 | 3 | 1 |
| β-strand | 148-149 | 2 | 1 |
| α-helix | 150-151 | 2 | |
| β-strand | 155 | 1 | 2 |
| α-helix | 157-159 | 3 | |
| β-strand | 166-169 | 4 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 202-206 | 5 | 3 |
| β-strand | 212-216 | 5 | 3 |
| β-strand | 222 | 1 | 4 |
| α-helix | 223-233 | 11 | |
| α-helix | 238-240 | 3 | |
| β-strand | 242-244 | 3 | 3 |
| β-strand | 249 | 1 | 3 |
| α-helix | 250-251 | 2 | |
| β-strand | 255 | 1 | 4 |
| β-strand | 266-270 | 5 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 320-329 | 10 | |
| α-helix | 333-348 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Unconventional myosin-VI | A, D | protein | 43 | Homo sapiens | Q9UM54 (AlphaFold model) |
| Ubiquitin | B | protein | 76 | Homo sapiens | P0CG47 (AlphaFold model) |
| Ubiquitin | C | protein | 76 | Homo sapiens | P0CG47 (AlphaFold model) |
>2N13_1 Unconventional myosin-VI (chains A, D) GTKKYDLSKWKYAELRDTINTSCDIELLAACREEFHRRLKVYH
>2N13_2 Ubiquitin (chains B) MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQRESTLHLVLRLRGG
>2N13_3 Ubiquitin (chains C) MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGC
Myosin VI Contains a Compact Structural Motif that Binds to Ubiquitin Chains. He, F., Wollscheid, H.P., Nowicka, U. et al. Cell Rep (2016) 14:2683-2694. DOI 10.1016/j.celrep.2016.01.079 · PubMed
Other PDB entries of the same protein (UniProt Q9UM54 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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