Crystal structure of S. pombe AMSH-like protease SST2 catalytic domain from P212121 space group. Determined by X-ray diffraction at 1.8 Å resolution. Released 18 Jun 2014.
Explore 4MSJ in 3D Show helices and sheets RCSB PDB PDBe
4MSJ contains 24 α-helices and 39 β-strands across 3 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 | 1 | 3 |
| β-strand | 319 | 1 | 3 |
| α-helix | 322-331 | 10 | |
| 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 |
|---|---|---|---|
| α-helix | 248-250 | 3 | |
| β-strand | 253 | 1 | 4 |
| β-strand | 259 | 1 | 4 |
| β-strand | 263-266 | 4 | 5 |
| α-helix | 269-276 | 8 | |
| α-helix | 278-282 | 5 | |
| β-strand | 288-296 | 9 | 5 |
| β-strand | 299-307 | 9 | 5 |
| β-strand | 310 | 1 | 6 |
| β-strand | 319 | 1 | 6 |
| α-helix | 323-331 | 9 | |
| α-helix | 334 | 1 | |
| β-strand | 335-342 | 8 | 5 |
| α-helix | 352-364 | 13 | |
| β-strand | 369-374 | 6 | 5 |
| α-helix | 375-377 | 3 | |
| β-strand | 379-385 | 7 | 5 |
| α-helix | 389-396 | 8 | |
| β-strand | 411-413 | 3 | 5 |
| α-helix | 414-415 | 2 | |
| β-strand | 420-423 | 4 | 5 |
| α-helix | 426-427 | 2 | |
| β-strand | 428-431 | 4 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 252-253 | 2 | 7 |
| β-strand | 259-260 | 2 | 7 |
| β-strand | 262-266 | 5 | 8 |
| α-helix | 269-276 | 8 | |
| α-helix | 278-282 | 5 | |
| β-strand | 288-296 | 9 | 8 |
| β-strand | 299-307 | 9 | 8 |
| β-strand | 310-312 | 3 | 9 |
| β-strand | 317-319 | 3 | 9 |
| α-helix | 323-331 | 9 | |
| α-helix | 334 | 1 | |
| β-strand | 335-342 | 8 | 8 |
| α-helix | 352-364 | 13 | |
| β-strand | 369-374 | 6 | 8 |
| α-helix | 375-377 | 3 | |
| β-strand | 379-385 | 7 | 8 |
| α-helix | 389-396 | 8 | |
| β-strand | 411-413 | 3 | 8 |
| α-helix | 414-415 | 2 | |
| β-strand | 420-423 | 4 | 8 |
| β-strand | 428-431 | 4 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| AMSH-like protease sst2 | A, B, C | protein | 197 | Schizosaccharomyces pombe | Q9P371 (AlphaFold model) |
>4MSJ_1 AMSH-like protease sst2 (chains A, B, C) GPLGSMAGTFKIHAYTEGGKPLRTIYLPKLLKKVFLDVVKPNTKKNLETCGILCGKLRQN AFFITHLVIPLQEATSDTCGTTDEASLFEFQDKHNLLTLGWIHTHPTQTCFMSSVDLHTH CSYQLMLPEAIAIVMAPSKNTSGIFRLLDPEGLQTIVKCRKPGLFHPHEGKVYTMVAQPG HVREINSKLQVVDLRVK
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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