4JXE: Schizosaccharomyces pombe sst2 catalytic domain

Crystal structure of Schizosaccharomyces pombe sst2 catalytic domain. Determined by X-ray diffraction at 1.45 Å resolution. Released 30 Apr 2014.

Method
X-ray diffraction
Resolution
1.45 Å
Organism
Schizosaccharomyces pombe
Chains
2
Atoms
3,274
Mol. weight
44.84 kDa
Ligands
ZN
Released
30 Apr 2014

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

Secondary structure: helices and β-sheets

4JXE contains 12 α-helices and 26 β-strands across 2 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
α-helix248-2503
β-strand25311
β-strand25911
β-strand263-26642
α-helix269-28214
β-strand288-29692
β-strand299-30792
β-strand31013
β-strand31913
α-helix323-3319
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: 6 helices, 13 β-strands
ElementResiduesLengthSheet
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
β-strand335-34285
α-helix352-36413
β-strand369-37465
β-strand379-38575
α-helix389-3968
β-strand411-41335
α-helix414-4152
β-strand420-42345
β-strand428-43145

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
AMSH-like protease sst2A, Bprotein197Schizosaccharomyces pombeQ9P371 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4JXE_1 AMSH-like protease sst2 (chains A, B)
GPLGSMAGTFKIHAYTEGGKPLRTIYLPKLLKKVFLDVVKPNTKKNLETCGILCGKLRQN
AFFITHLVIPLQEATSDTCGTTDEASLFEFQDKHNLLTLGWIHTHPTQTCFMSSVDLHTH
CSYQLMLPEAIAIVMAPSKNTSGIFRLLDPEGLQTIVKCRKPGLFHPHEGKVYTMVAQPG
HVREINSKLQVVDLRVK

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn4

Water and common crystallization additives (TRS, 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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