4MSD: AMSH-like protease sst2

Crystal structure of Schizosaccharomyces pombe AMSH-like protein SST2 T319I mutant. Determined by X-ray diffraction at 1.9 Å resolution. Released 18 Jun 2014.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Schizosaccharomyces pombe
Chains: 2
Atoms: 3,144
Mol. weight: 45.27 kDa
Ligands: ZN, DTT
Released: 18 Jun 2014

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

Secondary structure: helices and β-sheets

4MSD 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

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

Chain B: 6 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	252-253	2	4
β-strand	259-260	2	4
β-strand	263-266	4	5
α-helix	269-282	14
β-strand	288-296	9	5
β-strand	299-307	9	5
β-strand	310-312	3	6
β-strand	317-319	3	6
α-helix	322-331	10
α-helix	334	1
β-strand	335-342	8	5
α-helix	352-364	13
β-strand	369-374	6	5
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
β-strand	428-431	4	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
AMSH-like protease sst2	A, B	protein	197	Schizosaccharomyces pombe	Q9P371 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4MSD_1 AMSH-like protease sst2 (chains A, B)
GPLGSMAGTFKIHAYTEGGKPLRTIYLPKLLKKVFLDVVKPNTKKNLETCGILCGKLRQN
AFFITHLVIPLQEATSDTCGITDEASLFEFQDKHNLLTLGWIHTHPTQTCFMSSVDLHTH
CSYQLMLPEAIAIVMAPSKNTSGIFRLLDPEGLQTIVKCRKPGLFHPHEGKVYTMVAQPG
HVREINSKLQVVDLRVK

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	4
DTT	2,3-dihydroxy-1,4-dithiobutane	C4 H10 O2 S2	1

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:

4JXE 1.45 Å, Crystal structure of Schizosaccharomyces pombe sst2 catalytic domain
4K1R 1.63 Å, Crystal structure of Schizosaccharomyces pombe sst2 catalytic domain and Ubiquitin
4ZD4 1.63 Å, Catalytic domain of Sst2 F403W mutant
4MS7 1.67 Å, Crystal structure of Schizosaccharomyces pombe sst2 catalytic domain
4ZFR 1.72 Å, Catalytic domain of Sst2 F403A mutant bound to ubiquitin
4MSM 1.74 Å, Crystal structure of Schizosaccharomyces pombe AMSH-like protease sst2 E286A mutant…
4MSJ 1.8 Å, Crystal structure of S. pombe AMSH-like protease SST2 catalytic domain from P212121…
4MSQ 1.95 Å, Crystal structure of Schizosaccharomyces pombe AMSH-like protease sst2 catalytic domain…
4PQT 2.05 Å, Insights into the mechanism of deubiquitination by JAMM deubiquitinases from co-crystal…
4ZD5 2.07 Å, Catalytic domain of Sst2 F403A mutant
4NQL 2.3 Å, The crystal structure of the DUB domain of AMSH orthologue, Sst2 from S. pombe, in…
4ZFT 2.3 Å, Catalytic domain of Sst2 F403W mutant bound to ubiquitin

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