The structure of h/ceOTUB1-ubiquitin aldehyde-UBC13~Ub. Determined by X-ray diffraction at 3.11 Å resolution. Released 22 Feb 2012.
Explore 4DHZ in 3D Show helices and sheets RCSB PDB PDBe
4DHZ contains 29 α-helices and 36 β-strands across 4 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 | 23-27 | 5 | |
| α-helix | 29-40 | 12 | |
| β-strand | 44 | 1 | 1 |
| α-helix | 45-47 | 3 | |
| β-strand | 48-49 | 2 | 2 |
| α-helix | 51-54 | 4 | |
| α-helix | 63-75 | 13 | |
| β-strand | 76-80 | 5 | 2 |
| β-strand | 82 | 1 | 1 |
| α-helix | 88-101 | 14 | |
| α-helix | 105-124 | 20 | |
| α-helix | 129-148 | 20 | |
| α-helix | 153-159 | 7 | |
| α-helix | 163-183 | 21 | |
| α-helix | 185-188 | 4 | |
| α-helix | 189-191 | 3 | |
| α-helix | 198-201 | 4 | |
| α-helix | 202-206 | 5 | |
| β-strand | 213 | 1 | 3 |
| α-helix | 215-225 | 11 | |
| β-strand | 229-233 | 5 | 2 |
| β-strand | 244-248 | 5 | 2 |
| α-helix | 255-257 | 3 | |
| β-strand | 259-264 | 6 | 2 |
| β-strand | 266 | 1 | 3 |
| β-strand | 267-273 | 7 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 502-507 | 6 | 4 |
| β-strand | 511-516 | 6 | 4 |
| β-strand | 522 | 1 | 5 |
| α-helix | 523-533 | 11 | |
| α-helix | 538-540 | 3 | |
| β-strand | 541-545 | 5 | 4 |
| β-strand | 548-549 | 2 | 4 |
| β-strand | 555 | 1 | 5 |
| α-helix | 556-559 | 4 | |
| α-helix | 561-562 | 2 | |
| β-strand | 566-571 | 6 | 4 |
| β-strand | 575 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 502-506 | 5 | 6 |
| β-strand | 512-516 | 5 | 6 |
| β-strand | 522 | 1 | 7 |
| α-helix | 524-533 | 10 | |
| β-strand | 541-544 | 4 | 6 |
| β-strand | 549 | 1 | 6 |
| β-strand | 555 | 1 | 7 |
| α-helix | 557-559 | 3 | |
| β-strand | 566-571 | 6 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-17 | 12 | |
| β-strand | 20 | 1 | 8 |
| β-strand | 23-27 | 5 | 8 |
| β-strand | 34-40 | 7 | 8 |
| α-helix | 41-42 | 2 | |
| β-strand | 51-57 | 7 | 8 |
| α-helix | 66-67 | 2 | |
| β-strand | 68-71 | 4 | 8 |
| β-strand | 77 | 1 | 9 |
| β-strand | 80 | 1 | 9 |
| β-strand | 85 | 1 | 8 |
| β-strand | 86 | 1 | 9 |
| α-helix | 89-91 | 3 | |
| α-helix | 101-109 | 9 | |
| β-strand | 112 | 1 | 10 |
| β-strand | 115 | 1 | 10 |
| α-helix | 124-131 | 8 | |
| α-helix | 133-147 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin thioesterase otubain-like | A | protein | 288 | Homo sapiens, Caenorhabditis elegans | Q96FW1 (AlphaFold model), Q9XVR6 (AlphaFold model) |
| Ubiquitin aldehyde | B | protein | 76 | Homo sapiens | P0CG48 (AlphaFold model) |
| Ubiquitin | E | protein | 76 | Homo sapiens | P0CG48 (AlphaFold model) |
| Ubiquitin-conjugating enzyme E2 N | F | protein | 152 | Homo sapiens | P61088 (AlphaFold model) |
>4DHZ_1 Ubiquitin thioesterase otubain-like (chains A) MAAEEPQQQKQEPLGSDSEGVNCLAYDEAIMAQQDRIQQEIAVQNPLVATLAPFSILCAE YDNETSAAFLSKATELSEVYGEIRYIRGDGNCFYRAILVGLIEIMLKDRARLEKFIASSR DWTRTLVELGFPDWTCTDFCDFFIEFLEKIHSGVHTEEAVYTILNDDGSANYILMFFRLI TSAFLKQNSEEYAPFIDEGMTVAQYCEQEIEPMWKDADHLAINSLIKAAGTRVRIEYMDR TAAPNGGWHYDIPSDDQQIAPEITLLYRPGHYDVIYKKDSTEASEIEN
>4DHZ_2 Ubiquitin aldehyde (chains B) MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG
>4DHZ_3 Ubiquitin (chains E) MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGC
>4DHZ_4 Ubiquitin-conjugating enzyme E2 N (chains F) MAGLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGPQDSPFEGGTFKLELFLPE EYPMAAPKVRFMTKIYHPNVDKLGRICLDILKDKWSPALQIRTVLLSIQALLSAPNPDDP LANDVAEQWKTNEAQAIETARAWTRLYAMNNI
The mechanism of OTUB1-mediated inhibition of ubiquitination. Wiener, R., Zhang, X., Wang, T. et al. Nature (2012) 483:618-622. DOI 10.1038/nature10911 · PubMed
Other PDB entries of the same protein (UniProt Q96FW1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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