UCHL3 in complex with synthetic, K27-linked diubiquitin. Determined by X-ray diffraction at 2.1 Å resolution. Released 26 Feb 2020.
Explore 6QML in 3D Show helices and sheets RCSB PDB PDBe
6QML contains 38 α-helices and 56 β-strands across 6 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 | |
| α-helix | 108-110 | 3 | |
| β-strand | 113 | 1 | 3 |
| α-helix | 118-126 | 9 | |
| α-helix | 131-139 | 9 | |
| α-helix | 142-152 | 11 | |
| β-strand | 155 | 1 | 5 |
| β-strand | 168-176 | 9 | 4 |
| β-strand | 179-183 | 5 | 4 |
| β-strand | 191-195 | 5 | 4 |
| α-helix | 201-215 | 15 | |
| β-strand | 223-229 | 7 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 6 |
| β-strand | 12-16 | 5 | 6 |
| β-strand | 22 | 1 | 7 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 6 |
| β-strand | 48-49 | 2 | 6 |
| α-helix | 50-51 | 2 | |
| β-strand | 55 | 1 | 7 |
| α-helix | 57-59 | 3 | |
| β-strand | 66-71 | 6 | 6 |
| β-strand | 74-75 | 2 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 8 |
| β-strand | 12-16 | 5 | 8 |
| β-strand | 22 | 1 | 9 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 8 |
| β-strand | 48-49 | 2 | 8 |
| α-helix | 50-51 | 2 | |
| β-strand | 55 | 1 | 9 |
| α-helix | 57-59 | 3 | |
| β-strand | 66-71 | 6 | 8 |
| β-strand | 72 | 1 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5 | 1 | 10 |
| α-helix | 6-8 | 3 | |
| β-strand | 9-10 | 2 | 11 |
| α-helix | 13-22 | 10 | |
| β-strand | 25 | 1 | 12 |
| β-strand | 29-33 | 5 | 13 |
| α-helix | 39-42 | 4 | |
| β-strand | 49-57 | 9 | 13 |
| α-helix | 60-76 | 17 | |
| β-strand | 92 | 1 | 10 |
| α-helix | 95-105 | 11 | |
| α-helix | 108-110 | 3 | |
| β-strand | 113 | 1 | 12 |
| α-helix | 118-126 | 9 | |
| α-helix | 131-139 | 9 | |
| α-helix | 142-152 | 11 | |
| β-strand | 155 | 1 | 14 |
| α-helix | 158-161 | 4 | |
| α-helix | 165-166 | 2 | |
| β-strand | 168-176 | 9 | 13 |
| β-strand | 179-183 | 5 | 13 |
| β-strand | 191-195 | 5 | 13 |
| α-helix | 201-215 | 15 | |
| β-strand | 223-229 | 7 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 15 |
| β-strand | 12-15 | 4 | 15 |
| β-strand | 22 | 1 | 16 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 15 |
| β-strand | 48-49 | 2 | 15 |
| α-helix | 50-51 | 2 | |
| β-strand | 55 | 1 | 16 |
| α-helix | 57-59 | 3 | |
| β-strand | 66-71 | 6 | 15 |
| β-strand | 74-75 | 2 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin carboxyl-terminal hydrolase isozyme L3 | A, D | protein | 227 | Homo sapiens | P15374 (AlphaFold model) |
| Polyubiquitin-B | B, E | protein | 76 | Homo sapiens | P0CG47 (AlphaFold model) |
| Polyubiquitin-C | C, F | protein | 76 | Homo sapiens | P0CG48 (AlphaFold model) |
>6QML_1 Ubiquitin carboxyl-terminal hydrolase isozyme L3 (chains A, D) QRWLPLEANPEVTNQFLKQLGLHPNWQFVDVYGMDPELLSMVPRPVCAVLLLFPITEKYE VFRTEEEEKIKSQGQDVTSSVYFMKQTISNACGTIGLIHAIANNKDKMHFESGSTLKKFL EESVSMSPEERARYLENYDAIRVTHETSAHEGQTEAPSIDEKVDLHFIALVHVDGHLYEL DGRKPFPINHGETSDETLLEDAIEVCKKFMERDPDELRFNAIALSAA
>6QML_2 Polyubiquitin-B (chains B, E) LQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG
>6QML_3 Polyubiquitin-C (chains C, F) MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG
K27-Linked Diubiquitin Inhibits UCHL3 via an Unusual Kinetic Trap. van Tilburg, G.B.A., Murachelli, A.G., Fish, A. et al. Cell Chem Biol (2021) 28:191-201.e8. DOI 10.1016/j.chembiol.2020.11.005 · 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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