Crystal Structure of USP2 and a mutant form of Ubiquitin. Determined by X-ray diffraction at 2.1 Å resolution. Released 19 Dec 2012.
Explore 3V6E in 3D Show helices and sheets RCSB PDB PDBe
3V6E contains 20 α-helices and 28 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 | 268-269 | 2 | 1 |
| α-helix | 276-286 | 11 | |
| α-helix | 289-296 | 8 | |
| α-helix | 300-303 | 4 | |
| α-helix | 314-325 | 12 | |
| α-helix | 328-329 | 2 | |
| β-strand | 333-334 | 2 | 1 |
| α-helix | 337-346 | 10 | |
| α-helix | 348-350 | 3 | |
| α-helix | 358-373 | 16 | |
| α-helix | 392-404 | 13 | |
| α-helix | 410-415 | 6 | |
| β-strand | 417-425 | 9 | 2 |
| β-strand | 431-438 | 8 | 2 |
| β-strand | 441-443 | 3 | 3 |
| β-strand | 454 | 1 | 4 |
| α-helix | 455-463 | 9 | |
| β-strand | 466-468 | 3 | 2 |
| α-helix | 470-472 | 3 | |
| α-helix | 473-474 | 2 | |
| β-strand | 475-476 | 2 | 5 |
| β-strand | 481-482 | 2 | 5 |
| β-strand | 485-493 | 9 | 2 |
| β-strand | 497-502 | 6 | 3 |
| β-strand | 505-506 | 2 | 6 |
| β-strand | 513-514 | 2 | 6 |
| β-strand | 520 | 1 | 4 |
| β-strand | 526-527 | 2 | 3 |
| α-helix | 529-531 | 3 | |
| β-strand | 532 | 1 | 2 |
| β-strand | 540-550 | 11 | 3 |
| β-strand | 557-563 | 7 | 3 |
| β-strand | 570-574 | 5 | 3 |
| β-strand | 577-581 | 5 | 3 |
| α-helix | 583-585 | 3 | |
| β-strand | 591-598 | 8 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | -4--1 | 4 | |
| β-strand | 1-6 | 6 | 7 |
| β-strand | 12-17 | 6 | 7 |
| β-strand | 22 | 1 | 8 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 42-45 | 4 | 7 |
| β-strand | 48-49 | 2 | 7 |
| α-helix | 50 | 1 | |
| β-strand | 55 | 1 | 8 |
| α-helix | 57-59 | 3 | |
| β-strand | 66-70 | 5 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin carboxyl-terminal hydrolase 2 | A | protein | 367 | Homo sapiens | O75604 (AlphaFold model) |
| Ubiquitin | B | protein | 91 | Homo sapiens | P0CG48 (AlphaFold model) |
>3V6E_1 Ubiquitin carboxyl-terminal hydrolase 2 (chains A) MGSSHHHHHHSSGLVPRGSMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQR LYMRDLHHGSNAHTALVEEFAKLIQTIWTSSPNDVVSPSEFKTQIQRYAPRFVGYNQQDA QEFLRFLLDGLHNEVNRVTLRPKSNPENLDHLPDDEKGRQMWRKYLEREDSRIGDLFVGQ LKSSLTCTDCGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDVLDGDEKPTCCR CRGRKRCIKKFSIQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLRDLDLREFASENTNH AVYNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYEL ASPPSRM
>3V6E_2 Ubiquitin (chains B) MAHHHHHHSSGLVPRGSMQIFVNTLSGKHITLEVEPSDTIENVKAKIQDKEGIPPDQQRL IFAGKQLEDGRTLSDYNIQKESTLHLVLRLR
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
Water and common crystallization additives (GOL, CL) are not listed.
A strategy for modulation of enzymes in the ubiquitin system. Ernst, A., Avvakumov, G., Tong, J. et al. Science (2013) 339:590-595. DOI 10.1126/science.1230161 · PubMed
Other PDB entries of the same protein (UniProt O75604 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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