Crystal structure of mUCH37-hRPN13 CTD complex. Determined by X-ray diffraction at 2.85 Å resolution. Released 4 Mar 2015.
Explore 4WLQ in 3D Show helices and sheets RCSB PDB PDBe
4WLQ contains 25 α-helices and 11 β-strands across 2 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 | 15-24 | 10 | |
| β-strand | 28 | 1 | 1 |
| β-strand | 30-34 | 5 | 2 |
| β-strand | 49-56 | 8 | 2 |
| α-helix | 62-64 | 3 | |
| β-strand | 67-68 | 2 | 2 |
| α-helix | 69 | 1 | |
| α-helix | 73-76 | 4 | |
| α-helix | 85-87 | 3 | |
| α-helix | 88-97 | 10 | |
| β-strand | 106 | 1 | 1 |
| α-helix | 108-117 | 10 | |
| α-helix | 123-131 | 9 | |
| α-helix | 134-142 | 9 | |
| α-helix | 145-146 | 2 | |
| β-strand | 164-171 | 8 | 2 |
| β-strand | 174-178 | 5 | 2 |
| α-helix | 185 | 1 | |
| β-strand | 186-190 | 5 | 2 |
| α-helix | 197-213 | 17 | |
| β-strand | 218-225 | 8 | 2 |
| α-helix | 227-242 | 16 | |
| α-helix | 255-288 | 34 | |
| α-helix | 292-305 | 14 | |
| α-helix | 309-312 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 288-292 | 5 | |
| α-helix | 298-301 | 4 | |
| α-helix | 304-310 | 7 | |
| α-helix | 311-313 | 3 | |
| β-strand | 317 | 1 | 3 |
| β-strand | 320 | 1 | 3 |
| α-helix | 326-332 | 7 | |
| α-helix | 334-347 | 14 | |
| α-helix | 354-357 | 4 | |
| α-helix | 363-370 | 8 | |
| α-helix | 374-378 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin carboxyl-terminal hydrolase isozyme L5 | A | protein | 328 | Mus musculus | Q9WUP7 (AlphaFold model) |
| Proteasomal ubiquitin receptor ADRM1 | B | protein | 99 | Homo sapiens | Q16186 (AlphaFold model) |
>4WLQ_1 Ubiquitin carboxyl-terminal hydrolase isozyme L5 (chains A) MSSNAGEWCLMESDPGVFTELIKGFGCRGAQVEEIWSLEPESFEKLKPVHGLIFLFKWQP GEEPAGSVVQDSRLETIFFAKQVINNACATQAIVSVLLNCTHQDVHLGETLSEFKEFSQS FDAAMKGLALSNSDVIRQVHNSFARQQMFEFDTKTPAKEEDAFHFVSYVPVNGRLYELDG LREGPIDLGACNQDDWITAVRPVIEKRIQKYSEGEIRFNLMAIVSDRKMIYEQKIAELQR QLAEEPMDTDQGSTVLSAIQSEVARNQMLIEEEVQKLKRYKIENIRRKHNYLPFIMELLK TLAEHQQLIPLVEKAKEKQNAKKAQETK
>4WLQ_2 Proteasomal ubiquitin receptor ADRM1 (chains B) VDLASVLTPEIMAPILANADVQERLLPYLPSGESLPQTADEIQNTLTSPQFQQALGMFSA ALASGQLGPLMCQFGLPAEAVEAANKGDVEAFAKAMQNN
Structural Basis for the Activation and Inhibition of the UCH37 Deubiquitylase. VanderLinden, R.T., Hemmis, C.W., Schmitt, B. et al. Mol Cell (2015) 57:901-911. DOI 10.1016/j.molcel.2015.01.016 · PubMed
Other PDB entries of the same protein (UniProt Q9WUP7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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