Structure of the CYLD USP domain. Determined by X-ray diffraction at 2.8 Å resolution. Released 11 Mar 2008.
Explore 2VHF in 3D Show helices and sheets RCSB PDB PDBe
2VHF contains 47 α-helices and 49 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 | 584-586 | 3 | |
| β-strand | 589-590 | 2 | 1 |
| β-strand | 593-594 | 2 | 2 |
| α-helix | 595-596 | 2 | |
| α-helix | 601-611 | 11 | |
| β-strand | 614 | 1 | 3 |
| α-helix | 615-617 | 3 | |
| α-helix | 618-622 | 5 | |
| α-helix | 623-625 | 3 | |
| α-helix | 633-637 | 5 | |
| α-helix | 638-645 | 8 | |
| α-helix | 646-650 | 5 | |
| β-strand | 653-654 | 2 | 2 |
| α-helix | 656-669 | 14 | |
| α-helix | 682-686 | 5 | |
| α-helix | 687-694 | 8 | |
| α-helix | 696-698 | 3 | |
| β-strand | 700-704 | 5 | 4 |
| α-helix | 708-709 | 2 | |
| β-strand | 710-712 | 3 | 4 |
| β-strand | 715-716 | 2 | 1 |
| β-strand | 729 | 1 | 5 |
| α-helix | 730-741 | 12 | |
| β-strand | 743-745 | 3 | 4 |
| β-strand | 751-755 | 5 | 1 |
| α-helix | 756-757 | 2 | |
| β-strand | 770 | 1 | 5 |
| β-strand | 774-775 | 2 | 1 |
| α-helix | 778-780 | 3 | |
| β-strand | 781 | 1 | 4 |
| α-helix | 786 | 1 | |
| β-strand | 787 | 1 | 6 |
| α-helix | 788 | 1 | |
| β-strand | 794 | 1 | 6 |
| β-strand | 797-798 | 2 | 7 |
| α-helix | 800-802 | 3 | |
| β-strand | 815-816 | 2 | 7 |
| α-helix | 818-824 | 7 | |
| α-helix | 828-830 | 3 | |
| β-strand | 836-837 | 2 | 7 |
| α-helix | 838-839 | 2 | |
| α-helix | 858 | 1 | |
| β-strand | 859-868 | 10 | 1 |
| β-strand | 871-877 | 7 | 1 |
| β-strand | 885-889 | 5 | 1 |
| β-strand | 905-908 | 4 | 1 |
| α-helix | 911-914 | 4 | |
| α-helix | 920-925 | 6 | |
| α-helix | 928-930 | 3 | |
| α-helix | 935-940 | 6 | |
| β-strand | 942 | 1 | 1 |
| β-strand | 944-948 | 5 | 1 |
| α-helix | 950-952 | 3 | |
| β-strand | 953 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 589-590 | 2 | 8 |
| β-strand | 593-594 | 2 | 9 |
| α-helix | 601-611 | 11 | |
| β-strand | 614 | 1 | 10 |
| α-helix | 619-622 | 4 | |
| α-helix | 633-642 | 10 | |
| α-helix | 645-650 | 6 | |
| β-strand | 653-654 | 2 | 9 |
| α-helix | 657-669 | 13 | |
| α-helix | 682-689 | 8 | |
| β-strand | 700-704 | 5 | 11 |
| α-helix | 708-709 | 2 | |
| β-strand | 710-712 | 3 | 11 |
| β-strand | 715-716 | 2 | 8 |
| β-strand | 729 | 1 | 12 |
| α-helix | 730-740 | 11 | |
| β-strand | 743-745 | 3 | 11 |
| β-strand | 751-755 | 5 | 8 |
| α-helix | 756-757 | 2 | |
| β-strand | 770 | 1 | 12 |
| β-strand | 774-776 | 3 | 8 |
| α-helix | 778-780 | 3 | |
| β-strand | 781 | 1 | 11 |
| β-strand | 787 | 1 | 13 |
| β-strand | 794 | 1 | 13 |
| β-strand | 797-798 | 2 | 14 |
| α-helix | 800-802 | 3 | |
| α-helix | 813-814 | 2 | |
| β-strand | 815-816 | 2 | 14 |
| α-helix | 818-824 | 7 | |
| α-helix | 828-830 | 3 | |
| β-strand | 836-837 | 2 | 14 |
| α-helix | 844-846 | 3 | |
| β-strand | 858-868 | 11 | 8 |
| β-strand | 871-877 | 7 | 8 |
| β-strand | 885-889 | 5 | 8 |
| β-strand | 905-908 | 4 | 8 |
| α-helix | 912-915 | 4 | |
| α-helix | 921-923 | 3 | |
| α-helix | 936-940 | 5 | |
| β-strand | 942-948 | 7 | 8 |
| β-strand | 953 | 1 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin carboxyl-terminal hydrolase cyld | A, B | protein | 374 | HOMO SAPIENS | Q9NQC7 (AlphaFold model) |
>2VHF_1 UBIQUITIN CARBOXYL-TERMINAL HYDROLASE CYLD (chains A, B) GLEIMIGKKKGIQGHYNSCYLDSTLFCLFAFSSVLDTVLLRPKEKNDVEYYSETQELLRT EIVNPLRIYGYVCATKIMKLRKILEKVEAASGFTSEEKDPEEFLNILFHHILRVEPLLKI RSAGQKVQDCYFYQIFMEKNEKVGVPTIQQLLEWSFINSNLKFAEAPSCLIIQMPRFGKD FKLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYECRECYDDPDISAGKIKQFCKTCNT QVHLHPKRLNHKYNPVSLPKDLPDWDWRHGCIPCQNMELFAVLCIETSHYVAFVKYGKDD SAWLFFDSMADRDGGQNGFNIPQVTPCPEVGEYLKMSLEDLHSLDSRRIQGCARRLLCDA YMCMYQSPTMSLYK
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
The Structure of the Cyld Usp Domain Explains its Specificity for Lys63-Linked Polyubiquitin and Reveals a B-Box Module. Komander, D., Lord, C.J., Scheel, H. et al. Mol Cell Biol (2008) 29:451. DOI 10.1016/J.MOLCEL.2007.12.018 · 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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