Crystal structure of Schizosaccharomyces pombe AMSH-like protease sst2 E286A mutant bound to ubiquitin. Determined by X-ray diffraction at 1.74 Å resolution. Released 18 Jun 2014.
Explore 4MSM in 3D Show helices and sheets RCSB PDB PDBe
4MSM contains 20 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 | 322-332 | 11 | |
| β-strand | 335-342 | 8 | 2 |
| α-helix | 352-364 | 13 | |
| β-strand | 369-374 | 6 | 2 |
| α-helix | 375-377 | 3 | |
| 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 | 2-6 | 5 | 4 |
| β-strand | 12-16 | 5 | 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 |
| α-helix | 50-51 | 2 | |
| β-strand | 55 | 1 | 5 |
| α-helix | 57-59 | 3 | |
| 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 | 322-331 | 10 | |
| β-strand | 335-342 | 8 | 7 |
| α-helix | 352-364 | 13 | |
| β-strand | 369-374 | 6 | 7 |
| α-helix | 375-377 | 3 | |
| 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 |
| 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) |
>4MSM_1 AMSH-like protease sst2 (chains A, C) GPLGSMAGTFKIHAYTEGGKPLRTIYLPKLLKKVFLDVVKPNTKKNLATCGILCGKLRQN AFFITHLVIPLQEATSDTCGTTDEASLFEFQDKHNLLTLGWIHTHPTQTCFMSSVDLHTH CSYQLMLPEAIAIVMAPSKNTSGIFRLLDPEGLQTIVKCRKPGLFHPHEGKVYTMVAQPG HVREINSKLQVVDLRVK
>4MSM_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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