Solution structure of the C-terminal region in human tubulin folding cofactor C. Determined by solution NMR. Released 15 Apr 2008.
Explore 2YUH in 3D Show helices and sheets RCSB PDB PDBe
2YUH contains 2 α-helices and 20 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 |
|---|---|---|---|
| β-strand | 10-12 | 3 | 1 |
| β-strand | 17 | 1 | 2 |
| β-strand | 20-23 | 4 | 3 |
| α-helix | 25-28 | 4 | |
| β-strand | 32-35 | 4 | 1 |
| β-strand | 39 | 1 | 2 |
| β-strand | 42-45 | 4 | 3 |
| β-strand | 52-55 | 4 | 1 |
| β-strand | 58 | 1 | 4 |
| β-strand | 61-63 | 3 | 3 |
| β-strand | 71-74 | 4 | 1 |
| β-strand | 77 | 1 | 4 |
| β-strand | 80-82 | 3 | 3 |
| β-strand | 87-91 | 5 | 1 |
| β-strand | 94 | 1 | 4 |
| β-strand | 97-99 | 3 | 3 |
| β-strand | 105-109 | 5 | 1 |
| β-strand | 112 | 1 | 4 |
| β-strand | 114-117 | 4 | 3 |
| α-helix | 127-133 | 7 | |
| β-strand | 145-146 | 2 | 1 |
| β-strand | 160-161 | 2 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tubulin-specific chaperone C | A | protein | 179 | Homo sapiens | Q15814 (AlphaFold model) |
>2YUH_1 Tubulin-specific chaperone C (chains A) GSSGSSGSWVCGFSNLESQVLEKRASELHQRDVLLTELSNCTVRLYGNPNTLRLTKAHSC KLLCGPVSTSVFLEDCSDCVLAVACQQLRIHSTKDTRIFLQVTSRAIVEDCSGIQFAPYT WSYPEIDKDFESSGLDRSKNNWNDVDDFNWLARDMASPNWSILPEEERNIQWDSGPSSG
Solution structure of the C-terminal region in human tubulin folding cofactor C. Saito, K., Tochio, N., Kigawa, T. et al. To be published.
Other PDB entries of the same protein (UniProt Q15814 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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