Crystal structure of Schizosaccharomyces pombe AMSH-like protease sst2 catalytic domain bound to ubiquitin. Determined by X-ray diffraction at 1.95 Å resolution. Released 18 Jun 2014.
Explore 4MSQ in 3D Show helices and sheets RCSB PDB PDBe
4MSQ contains 17 α-helices and 42 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 |
|---|---|---|---|
| β-strand | 252-253 | 2 | 1 |
| β-strand | 259-260 | 2 | 1 |
| β-strand | 263-266 | 4 | 2 |
| α-helix | 269-282 | 14 | |
| β-strand | 288-296 | 9 | 2 |
| β-strand | 299-307 | 9 | 2 |
| β-strand | 310-312 | 3 | 3 |
| β-strand | 317-319 | 3 | 3 |
| α-helix | 322-331 | 10 | |
| α-helix | 334 | 1 | |
| β-strand | 335-342 | 8 | 2 |
| α-helix | 352-364 | 13 | |
| β-strand | 369-374 | 6 | 2 |
| β-strand | 379-385 | 7 | 2 |
| α-helix | 389-396 | 8 | |
| β-strand | 411-413 | 3 | 2 |
| α-helix | 414-415 | 2 | |
| β-strand | 420-423 | 4 | 2 |
| β-strand | 428-431 | 4 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1-6 | 6 | 4 |
| β-strand | 12-17 | 6 | 4 |
| β-strand | 22 | 1 | 5 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 4 |
| β-strand | 48-49 | 2 | 4 |
| β-strand | 55 | 1 | 5 |
| α-helix | 61-62 | 2 | |
| β-strand | 66-71 | 6 | 4 |
| β-strand | 74-75 | 2 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 252-253 | 2 | 6 |
| β-strand | 259-260 | 2 | 6 |
| β-strand | 263-266 | 4 | 7 |
| α-helix | 269-282 | 14 | |
| β-strand | 288-296 | 9 | 7 |
| β-strand | 299-307 | 9 | 7 |
| β-strand | 310-312 | 3 | 8 |
| β-strand | 317-319 | 3 | 8 |
| α-helix | 322-332 | 11 | |
| α-helix | 334 | 1 | |
| β-strand | 335-342 | 8 | 7 |
| α-helix | 352-364 | 13 | |
| β-strand | 369-374 | 6 | 7 |
| β-strand | 379-385 | 7 | 7 |
| α-helix | 389-396 | 8 | |
| β-strand | 411-413 | 3 | 7 |
| α-helix | 414-415 | 2 | |
| β-strand | 420-423 | 4 | 7 |
| β-strand | 428-431 | 4 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 9 |
| β-strand | 12-15 | 4 | 9 |
| β-strand | 22 | 1 | 10 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 9 |
| β-strand | 48-49 | 2 | 9 |
| β-strand | 55 | 1 | 10 |
| β-strand | 66-71 | 6 | 9 |
| β-strand | 74-75 | 2 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| AMSH-like protease sst2 | A, C | protein | 197 | Schizosaccharomyces pombe | Q9P371 (AlphaFold model) |
| Ubiquitin | B, D | protein | 81 | Homo sapiens | P0CG48 (AlphaFold model) |
>4MSQ_1 AMSH-like protease sst2 (chains A, C) GPLGSMAGTFKIHAYTEGGKPLRTIYLPKLLKKVFLDVVKPNTKKNLETCGILCGKLRQN AFFITHLVIPLQEATSDTCGTTDEASLFEFQDKHNLLTLGWIHTHPTQTCFMSSVDLHTH CSYQLMLPEAIAIVMAPSKNTSGIFRLLDPEGLQTIVKCRKPGLFHPHEGKVYTMVAQPG HVREINSKLQVVDLRVK
>4MSQ_2 Ubiquitin (chains B, D) GPLGSMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRT LSDYNIQKESTLHLVLRLRGG
Water and common crystallization additives (EDO) are not listed.
Insights into the Mechanism of Deubiquitination by JAMM Deubiquitinases from Cocrystal Structures of the Enzyme with the Substrate and Product. Shrestha, R.K., Ronau, J.A., Davies, C.W. et al. Biochemistry (2014) 53:3199-3217. DOI 10.1021/bi5003162 · PubMed
Other PDB entries of the same protein (UniProt Q9P371 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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