4MSJ: AMSH-like protease sst2

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.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Schizosaccharomyces pombe
Chains
3
Atoms
4,712
Mol. weight
67.19 kDa
Ligands
ZN, GLY, PO4
Released
18 Jun 2014

Explore 4MSJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 6 helices, 13 β-strands

ElementResiduesLengthSheet
β-strand252-25321
β-strand259-26021
β-strand263-26642
α-helix269-28214
β-strand288-29692
β-strand299-30792
β-strand31013
β-strand31913
α-helix322-33110
β-strand335-34282
α-helix352-36413
β-strand369-37462
α-helix375-3773
β-strand379-38572
α-helix389-3968
β-strand411-41332
α-helix414-4152
β-strand420-42342
β-strand428-43142
Chain B: 10 helices, 13 β-strands
ElementResiduesLengthSheet
α-helix248-2503
β-strand25314
β-strand25914
β-strand263-26645
α-helix269-2768
α-helix278-2825
β-strand288-29695
β-strand299-30795
β-strand31016
β-strand31916
α-helix323-3319
α-helix3341
β-strand335-34285
α-helix352-36413
β-strand369-37465
α-helix375-3773
β-strand379-38575
α-helix389-3968
β-strand411-41335
α-helix414-4152
β-strand420-42345
α-helix426-4272
β-strand428-43145
Chain C: 8 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand252-25327
β-strand259-26027
β-strand262-26658
α-helix269-2768
α-helix278-2825
β-strand288-29698
β-strand299-30798
β-strand310-31239
β-strand317-31939
α-helix323-3319
α-helix3341
β-strand335-34288
α-helix352-36413
β-strand369-37468
α-helix375-3773
β-strand379-38578
α-helix389-3968
β-strand411-41338
α-helix414-4152
β-strand420-42348
β-strand428-43148

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
AMSH-like protease sst2A, B, Cprotein197Schizosaccharomyces pombeQ9P371 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>4MSJ_1 AMSH-like protease sst2 (chains A, B, C)
GPLGSMAGTFKIHAYTEGGKPLRTIYLPKLLKKVFLDVVKPNTKKNLETCGILCGKLRQN
AFFITHLVIPLQEATSDTCGTTDEASLFEFQDKHNLLTLGWIHTHPTQTCFMSSVDLHTH
CSYQLMLPEAIAIVMAPSKNTSGIFRLLDPEGLQTIVKCRKPGLFHPHEGKVYTMVAQPG
HVREINSKLQVVDLRVK

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn6
GLYGlycineC2 H5 N O21
PO4Phosphate ionO4 P3

Water and common crystallization additives (EDO) are not listed.

Primary citation

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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