Crystal structure of Lys27-linked di-ubiquitin in complex with its selective interacting protein UCHL3. Determined by X-ray diffraction at 1.87 Å resolution. Released 6 Feb 2019.
Explore 6ISU in 3D Show helices and sheets RCSB PDB PDBe
6ISU contains 20 α-helices and 26 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 |
|---|---|---|---|
| β-strand | 5 | 1 | 1 |
| α-helix | 6-8 | 3 | |
| β-strand | 9-10 | 2 | 2 |
| α-helix | 13-22 | 10 | |
| β-strand | 25 | 1 | 3 |
| β-strand | 29-33 | 5 | 4 |
| α-helix | 39-42 | 4 | |
| β-strand | 49-57 | 9 | 4 |
| α-helix | 60-76 | 17 | |
| β-strand | 92 | 1 | 1 |
| α-helix | 95-105 | 11 | |
| β-strand | 113 | 1 | 3 |
| α-helix | 118-126 | 9 | |
| α-helix | 131-140 | 10 | |
| α-helix | 142-152 | 11 | |
| α-helix | 158-161 | 4 | |
| β-strand | 168-176 | 9 | 4 |
| β-strand | 179-183 | 5 | 4 |
| β-strand | 191-195 | 5 | 4 |
| α-helix | 198-200 | 3 | |
| α-helix | 201-214 | 14 | |
| β-strand | 223-229 | 7 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 5 |
| β-strand | 12-16 | 5 | 5 |
| β-strand | 22 | 1 | 6 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 5 |
| β-strand | 48-49 | 2 | 5 |
| α-helix | 50-51 | 2 | |
| β-strand | 55 | 1 | 6 |
| α-helix | 57-59 | 3 | |
| β-strand | 66-71 | 6 | 5 |
| α-helix | 72-74 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 7 |
| β-strand | 12-16 | 5 | 7 |
| β-strand | 22 | 1 | 8 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 7 |
| β-strand | 48-49 | 2 | 7 |
| β-strand | 55 | 1 | 8 |
| α-helix | 57-59 | 3 | |
| α-helix | 61-62 | 2 | |
| β-strand | 66-71 | 6 | 7 |
| β-strand | 74-75 | 2 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin carboxyl-terminal hydrolase isozyme L3 | A | protein | 230 | Homo sapiens | P15374 (AlphaFold model) |
| Ubiquitin | B | protein | 76 | Homo sapiens | P0CG47 (AlphaFold model) |
| Ubiquitin | C | protein | 76 | Homo sapiens | P0CG47 (AlphaFold model) |
>6ISU_1 Ubiquitin carboxyl-terminal hydrolase isozyme L3 (chains A) MEGQRWLPLEANPEVTNQFLKQLGLHPNWQFVDVYGMDPELLSMVPRPVCAVLLLFPITE KYEVFRTEEEEKIKSQGQDVTSSVYFMKQTISNACGTIGLIHAIANNKDKMHFESGSTLK KFLEESVSMSPEERARYLENYDAIRVTHETSAHEGQTEAPSIDEKVDLHFIALVHVDGHL YELDGRKPFPINHGETSDETLLEDAIEVCKKFMERDPDELRFNAIALSAA
>6ISU_2 Ubiquitin (chains B) MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG
>6ISU_3 Ubiquitin (chains C) MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG
Chemical Protein Synthesis Enabled Mechanistic Studies on the Molecular Recognition of K27-linked Ubiquitin Chains. Pan, M., Zheng, Q., Ding, S. et al. Angew Chem Int Ed Engl (2019) 58:2627-2631. DOI 10.1002/anie.201810814 · PubMed
Other PDB entries of the same protein (UniProt P15374 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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