4MSQ: AMSH-like protease sst2

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.

Method
X-ray diffraction
Resolution
1.95 Å
Organisms
Schizosaccharomyces pombe, Homo sapiens
Chains
4
Atoms
4,474
Mol. weight
63.1 kDa
Ligands
PO4, ZN
Released
18 Jun 2014

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

Secondary structure: helices and β-sheets

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.

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-strand310-31233
β-strand317-31933
α-helix322-33110
α-helix3341
β-strand335-34282
α-helix352-36413
β-strand369-37462
β-strand379-38572
α-helix389-3968
β-strand411-41332
α-helix414-4152
β-strand420-42342
β-strand428-43142
Chain B: 3 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand1-664
β-strand12-1764
β-strand2215
α-helix23-3412
α-helix38-403
β-strand41-4554
β-strand48-4924
β-strand5515
α-helix61-622
β-strand66-7164
β-strand74-7523
Chain C: 6 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand252-25326
β-strand259-26026
β-strand263-26647
α-helix269-28214
β-strand288-29697
β-strand299-30797
β-strand310-31238
β-strand317-31938
α-helix322-33211
α-helix3341
β-strand335-34287
α-helix352-36413
β-strand369-37467
β-strand379-38577
α-helix389-3968
β-strand411-41337
α-helix414-4152
β-strand420-42347
β-strand428-43147
Chain D: 2 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand3-759
β-strand12-1549
β-strand22110
α-helix23-3412
α-helix38-403
β-strand41-4559
β-strand48-4929
β-strand55110
β-strand66-7169
β-strand74-7528

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
AMSH-like protease sst2A, Cprotein197Schizosaccharomyces pombeQ9P371 (AlphaFold model)
UbiquitinB, Dprotein81Homo sapiensP0CG48 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>4MSQ_1 AMSH-like protease sst2 (chains A, C)
GPLGSMAGTFKIHAYTEGGKPLRTIYLPKLLKKVFLDVVKPNTKKNLETCGILCGKLRQN
AFFITHLVIPLQEATSDTCGTTDEASLFEFQDKHNLLTLGWIHTHPTQTCFMSSVDLHTH
CSYQLMLPEAIAIVMAPSKNTSGIFRLLDPEGLQTIVKCRKPGLFHPHEGKVYTMVAQPG
HVREINSKLQVVDLRVK
Sequence of entity 2 (B, D), FASTA
>4MSQ_2 Ubiquitin (chains B, D)
GPLGSMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRT
LSDYNIQKESTLHLVLRLRGG

Ligands and cofactors

IDNameFormulaCopies
PO4Phosphate ionO4 P1
ZNZinc ionZn4

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:

Browse structure collections

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