3VON: Crystalstructure of the ubiquitin protease
Crystalstructure of the ubiquitin protease. Determined by X-ray diffraction at 3.15 Å resolution. Released 30 May 2012.
- Method
- X-ray diffraction
- Resolution
- 3.15 Å
- Organism
- Homo sapiens
- Chains
- 42
- Atoms
- 51,450
- Mol. weight
- 742.23 kDa
- Released
- 30 May 2012
Explore 3VON in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3VON contains 362 α-helices and 350 β-strands across 42 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.
Chain a: 7 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-24 | 14 | |
| β-strand | 31-35 | 5 | 3 |
| β-strand | 45-51 | 7 | 3 |
| α-helix | 52-53 | 2 | |
| β-strand | 62-68 | 7 | 3 |
| α-helix | 77-78 | 2 | |
| β-strand | 79-82 | 4 | 3 |
| β-strand | 84 | 1 | 4 |
| β-strand | 91 | 1 | 5 |
| β-strand | 97 | 1 | 3 |
| β-strand | 98 | 1 | 5 |
| α-helix | 100-102 | 3 | |
| α-helix | 104-107 | 4 | |
| α-helix | 115-125 | 11 | |
| α-helix | 135-138 | 4 | |
| β-strand | 142 | 1 | 4 |
Chain A: 13 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 48 | 1 | 1 |
| β-strand | 52-53 | 2 | 2 |
| α-helix | 54-59 | 6 | |
| α-helix | 70-76 | 7 | |
| β-strand | 81-83 | 3 | 2 |
| β-strand | 85 | 1 | 1 |
| α-helix | 91-103 | 13 | |
| α-helix | 108-126 | 19 | |
| α-helix | 132-150 | 19 | |
| α-helix | 155-162 | 8 | |
| α-helix | 165-185 | 21 | |
| α-helix | 187-190 | 4 | |
| α-helix | 191-193 | 3 | |
| α-helix | 200-203 | 4 | |
| α-helix | 204-208 | 5 | |
| α-helix | 217-227 | 11 | |
| β-strand | 231-235 | 5 | 2 |
| β-strand | 247-249 | 3 | 2 |
| α-helix | 254-255 | 2 | |
| β-strand | 257-262 | 6 | 2 |
| β-strand | 265-269 | 5 | 2 |
Chain b: 8 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-17 | 12 | |
| α-helix | 19-20 | 2 | |
| β-strand | 23-28 | 6 | 9 |
| β-strand | 31-40 | 10 | 9 |
| α-helix | 41-42 | 2 | |
| β-strand | 51-57 | 7 | 9 |
| α-helix | 66-67 | 2 | |
| β-strand | 68-71 | 4 | 9 |
| β-strand | 77 | 1 | 10 |
| β-strand | 80 | 1 | 10 |
| β-strand | 85 | 1 | 9 |
| β-strand | 86 | 1 | 10 |
| α-helix | 89-91 | 3 | |
| α-helix | 101-113 | 13 | |
| α-helix | 126-131 | 6 | |
| α-helix | 133-147 | 15 | |
Chain B: 7 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-10 | 3 | |
| α-helix | 11-24 | 14 | |
| β-strand | 31-32 | 2 | 6 |
| β-strand | 35 | 1 | 6 |
| β-strand | 45-51 | 7 | 6 |
| α-helix | 52-53 | 2 | |
| β-strand | 62-68 | 7 | 6 |
| α-helix | 77-78 | 2 | |
| β-strand | 79-82 | 4 | 6 |
| β-strand | 84 | 1 | 7 |
| β-strand | 91 | 1 | 8 |
| β-strand | 97 | 1 | 6 |
| β-strand | 98 | 1 | 8 |
| α-helix | 104-107 | 4 | |
| α-helix | 115-125 | 11 | |
| α-helix | 137-138 | 2 | |
| β-strand | 142 | 1 | 7 |
Chain c: 13 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 48 | 1 | 13 |
| β-strand | 52-53 | 2 | 14 |
| α-helix | 54-59 | 6 | |
| α-helix | 69-76 | 8 | |
| β-strand | 81-83 | 3 | 14 |
| β-strand | 85 | 1 | 13 |
| α-helix | 91-103 | 13 | |
| α-helix | 108-127 | 20 | |
| α-helix | 132-150 | 19 | |
| α-helix | 155-159 | 5 | |
| α-helix | 165-185 | 21 | |
| α-helix | 187-190 | 4 | |
| α-helix | 191-193 | 3 | |
| α-helix | 200-203 | 4 | |
| α-helix | 204-208 | 5 | |
| α-helix | 217-227 | 11 | |
| β-strand | 231-235 | 5 | 14 |
| β-strand | 245-249 | 5 | 14 |
| α-helix | 254-255 | 2 | |
| β-strand | 257-262 | 6 | 14 |
| β-strand | 265-269 | 5 | 14 |
Chain C: 10 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-17 | 12 | |
| α-helix | 19-20 | 2 | |
| β-strand | 23-27 | 5 | 11 |
| α-helix | 28 | 1 | |
| β-strand | 34-40 | 7 | 11 |
| α-helix | 41-42 | 2 | |
| β-strand | 51-57 | 7 | 11 |
| α-helix | 66-67 | 2 | |
| β-strand | 68-71 | 4 | 11 |
| β-strand | 80 | 1 | 12 |
| β-strand | 85 | 1 | 11 |
| β-strand | 86 | 1 | 12 |
| α-helix | 89-91 | 3 | |
| α-helix | 101-113 | 13 | |
| α-helix | 124-130 | 7 | |
| α-helix | 133-143 | 11 | |
| α-helix | 144-148 | 5 | |
Chain d: 7 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-24 | 14 | |
| β-strand | 31-32 | 2 | 18 |
| β-strand | 35 | 1 | 18 |
| β-strand | 45-51 | 7 | 18 |
| α-helix | 52-53 | 2 | |
| β-strand | 62-68 | 7 | 18 |
| α-helix | 77-78 | 2 | |
| β-strand | 79-82 | 4 | 18 |
| β-strand | 84 | 1 | 19 |
| β-strand | 91 | 1 | 20 |
| β-strand | 97 | 1 | 18 |
| β-strand | 98 | 1 | 20 |
| α-helix | 99 | 1 | |
| α-helix | 115-125 | 11 | |
| α-helix | 129-132 | 4 | |
| α-helix | 137-138 | 2 | |
| β-strand | 142 | 1 | 19 |
Chain D: 7 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-10 | 3 | |
| α-helix | 11-24 | 14 | |
| β-strand | 31-35 | 5 | 15 |
| β-strand | 45-51 | 7 | 15 |
| α-helix | 52-53 | 2 | |
| β-strand | 62-68 | 7 | 15 |
| β-strand | 79-82 | 4 | 15 |
| β-strand | 84 | 1 | 16 |
| β-strand | 91 | 1 | 17 |
| β-strand | 97 | 1 | 15 |
| β-strand | 98 | 1 | 17 |
| α-helix | 100-102 | 3 | |
| α-helix | 104-107 | 4 | |
| α-helix | 115-125 | 11 | |
| α-helix | 137-138 | 2 | |
| β-strand | 142 | 1 | 16 |
32 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Ubiquitin thioesterase OTUB1 | A, H, O, V, c, j | protein | 228 | Homo sapiens | Q96FW1 (AlphaFold model) |
| Ubiquitin-conjugating enzyme E2 variant 2 | B, D, F, I, K, M, P, R, T, W, Y, a, d, f, h, k, m, o | protein | 138 | Homo sapiens | Q15819 (AlphaFold model) |
| Ubiquitin-conjugating enzyme E2 N | C, E, G, J, L, N, Q, S, U, X, Z, b, e, g, i, l, n, p | protein | 148 | Homo sapiens | P61088 (AlphaFold model) |
Sequence of entity 1 (A, H, O, V, c, j), FASTA
>3VON_1 Ubiquitin thioesterase OTUB1 (chains A, H, O, V, c, j)
SNPLVSERLELSVLYKEYAEDDNIYQQKIKDLHKKYSYIRKTRPDGNCFYRAFGFSHLEA
LLDDSKELQRFKAVSAKSKEDLVSQGFTEFTIEDFHNTFMDLIEQVEKQTSVADLLASFN
DQSTSDYLVVYLRLLTSGYLQRESKFFEHFIEGGRTVKEFCQQEVEPMCKESDHIHIIAL
AQALSVSIQVEYMDRGEGGTTNPHIFPEGSEPKVYLLYRPGHYDILYK
Sequence of entity 2 (B, D, F, I, K, M, P, R, T, W, Y, a, d, f, h, k, m, o), FASTA
>3VON_2 Ubiquitin-conjugating enzyme E2 variant 2 (chains B, D, F, I, K, M, P, R, T, W, Y, a, d, f, h, k, m, o)
GVKVPRNFRLLEELEEGQKGVGDGTVSWGLEDDEDMTLTRWTGMIIGPPRTNYENRIYSL
KVECGPKYPEAPPSVRFVTKINMNGINNSSGMVDARSIPVLAKWQNSYSIKVVLQELRRL
MMSKENMKLPQPPEGQTY
Sequence of entity 3 (C, E, G, J, L, N, Q, S, U, X, Z, b, e, g, i, l, n, p), FASTA
>3VON_3 Ubiquitin-conjugating enzyme E2 N (chains C, E, G, J, L, N, Q, S, U, X, Z, b, e, g, i, l, n, p)
GLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGPQDSPFEGGTFKLELFLPEEY
PMAAPKVRFMTKIYHPNVDKLGRICLDILKDKWSPALQIRTVLLSIQALLSAPNPDDPLA
NDVAEQWKTNEAQAIETARAWTRLYAMN
Primary citation
Molecular basis of Lys-63-linked polyubiquitination inhibition by the interaction between human deubiquitinating enzyme OTUB1 and ubiquitin-conjugating enzyme UBC13. Sato, Y., Yamagata, A., Goto-Ito, S. et al. J Biol Chem (2012) 287:25860-25868. DOI 10.1074/jbc.M112.364752 · PubMed
Other PDB entries of the same protein (UniProt Q96FW1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 2ZFY 1.69 Å, Crystal structure of human Otubain 1
- 4LDT 1.9 Å, The structure of h/ceOTUB1-ubiquitin aldehyde-UBCH5B~Ub
- 4I6L 2.49 Å, Crystal structure of OTUB1 in complex with ubiquitin variant
- 4DHZ 3.11 Å, The structure of h/ceOTUB1-ubiquitin aldehyde-UBC13~Ub
- 4DDG 3.3 Å, Crystal structure of human OTUB1/UbcH5b~Ub/Ub
- 4DDI 3.8 Å, Crystal structure of human OTUB1/UbcH5b~Ub/Ub
Browse structure collections
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