Solution structure of a Ubiquitin/UIM fusion protein. Determined by solution NMR. Released 9 Feb 2010.
Explore 2KDI in 3D Show helices and sheets RCSB PDB PDBe
2KDI contains 6 α-helices and 8 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 | 11-16 | 6 | 1 |
| β-strand | 21-25 | 5 | 1 |
| β-strand | 31 | 1 | 2 |
| α-helix | 32-43 | 12 | |
| α-helix | 47-49 | 3 | |
| β-strand | 50-52 | 3 | 1 |
| β-strand | 53-54 | 2 | 3 |
| β-strand | 57-58 | 2 | 3 |
| α-helix | 59-60 | 2 | |
| β-strand | 64 | 1 | 2 |
| β-strand | 75-80 | 6 | 1 |
| α-helix | 95-102 | 8 | |
| α-helix | 106-110 | 5 | |
| α-helix | 111-113 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin, Vacuolar protein sorting-associated protein 27 fusion protein | A | protein | 114 | Saccharomyces cerevisiae | P40343 (AlphaFold model) |
>2KDI_1 Ubiquitin, Vacuolar protein sorting-associated protein 27 fusion protein (chains A) MHHHHHHGEFQIFAKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIWAGKQLE DGRTLSDYNIQRESTLHLVLRLRGGSMGGAADEEELIRKAIELSLKESRNSGGY
Conformational Dynamics and Structural Plasticity Play Critical Roles in the Ubiquitin Recognition of a UIM Domain. Sgourakis, N.G., Patel, M.M., Garcia, A.E. et al. J Mol Biol (2010) 396:1128-1144. DOI 10.1016/j.jmb.2009.12.052 · PubMed
Other PDB entries of the same protein (UniProt P40343 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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