Structure of CYLD CAP-Gly3 (467-552) bound to Ub; tetragonal space group. Determined by X-ray diffraction at 1.71 Å resolution. Released 20 Oct 2021.
Explore 7OWD in 3D Show helices and sheets RCSB PDB PDBe
7OWD contains 4 α-helices and 16 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 |
|---|---|---|---|
| β-strand | 2-7 | 6 | 1 |
| β-strand | 12-16 | 5 | 1 |
| β-strand | 22 | 1 | 4 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 1 |
| β-strand | 48-49 | 2 | 1 |
| β-strand | 55 | 1 | 4 |
| α-helix | 57-59 | 3 | |
| β-strand | 66-71 | 6 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 474 | 1 | 1 |
| β-strand | 475-478 | 4 | 2 |
| β-strand | 484-492 | 9 | 2 |
| β-strand | 501-506 | 6 | 2 |
| β-strand | 514 | 1 | 2 |
| β-strand | 517-518 | 2 | 3 |
| β-strand | 521-522 | 2 | 3 |
| β-strand | 531-535 | 5 | 2 |
| α-helix | 536-538 | 3 | |
| β-strand | 540-541 | 2 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin carboxyl-terminal hydrolase CYLD | B | protein | 86 | Homo sapiens | Q9NQC7 (AlphaFold model) |
| Ubiquitin | A | protein | 76 | Homo sapiens | P0CG48 (AlphaFold model) |
>7OWD_1 Ubiquitin carboxyl-terminal hydrolase CYLD (chains B) SHGLEVGSLAEVKENPPFYGVIRWIGQPPGLNEVLAGLELEDECAGCTDGTFRGTRYFTC ALKKALFVKLKSCRPDSRFASLQPVS
>7OWD_2 Ubiquitin (chains A) MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG
Regulation of CYLD activity and specificity by phosphorylation and ubiquitin-binding CAP-Gly domains. Elliott, P.R., Leske, D., Wagstaff, J. et al. Cell Rep (2021) 37:109777-109777. DOI 10.1016/j.celrep.2021.109777 · PubMed
Other PDB entries of the same protein (UniProt Q9NQC7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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