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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：Q70CQ3 New Search
8PDB entries
9Biological assembly
34chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
5OHK Crystal structure of USP30 in covalent complex with ubiquitin propargylamide (high resolution) Deposited 2017-07-17 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 64–178（115 aa） Fragment：UNP residues 64-178,UNP residues 217-357,UNP residues 432-502
Chain A 217–357（141 aa） Fragment：UNP residues 64-178,UNP residues 217-357,UNP residues 432-502
Chain A 432–502（71 aa） Fragment：UNP residues 64-178,UNP residues 217-357,UNP residues 432-502
Mutation：;construct 13 (R179G, Q180S, P181G, R182S, F348D, M350S, I353E, L358S, L359N, G360A),construct 13 (R179G, Q180S, P181G, R182S, F348D, M350S, I353E, L358S, L359N, G360A),construct 13 (R179G, Q180S, P181G, R182S, F348D, M350S, I353E, L358S, L359N, G360A) ; Mutation：;construct 13 (R179G, Q180S, P181G, R182S, F348D, M350S, I353E, L358S, L359N, G360A),construct 13 (R179G, Q180S, P181G, R182S, F348D, M350S, I353E, L358S, L359N, G360A),construct 13 (R179G, Q180S, P181G, R182S, F348D, M350S, I353E, L358S, L359N, G360A) ; Mutation：;construct 13 (R179G, Q180S, P181G, R182S, F348D, M350S, I353E, L358S, L359N, G360A),construct 13 (R179G, Q180S, P181G, R182S, F348D, M350S, I353E, L358S, L359N, G360A),construct 13 (R179G, Q180S, P181G, R182S, F348D, M350S, I353E, L358S, L359N, G360A) ; ZN ZINC ION × 1 AYE prop-2-en-1-amine × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.4；291 K；10% (w/v) PEG 20000, 0.1 M sodium citrate pH 5.4, 0.2 M lithium sulfate
Resolution 2.34 Å R-free 0.261
5OHN Crystal structure of USP30 in covalent complex with ubiquitin propargylamide (low resolution) Deposited 2017-07-17 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 64–357（294 aa） Fragment：UNP residues 64-360,UNP residues 432-502
Chain A 432–502（71 aa） Fragment：UNP residues 64-360,UNP residues 432-502
Mutation：construct 8 (F348D, M350D, I353E, L358S, L359N, G360A),construct 8 (F348D, M350D, I353E, L358S, L359N, G360A) Mutation：construct 8 (F348D, M350D, I353E, L358S, L359N, G360A),construct 8 (F348D, M350D, I353E, L358S, L359N, G360A) ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；291 K；20% (w/v) PAA 5100 Na, 100 mM Hepes pH 8.0, 2.5% (v/v) glycerol
Resolution 3.60 Å R-free 0.253
5OHN Crystal structure of USP30 in covalent complex with ubiquitin propargylamide (low resolution) Deposited 2017-07-17 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain C 64–357（294 aa） Fragment：UNP residues 64-360,UNP residues 432-502
Chain C 432–502（71 aa） Fragment：UNP residues 64-360,UNP residues 432-502
Mutation：construct 8 (F348D, M350D, I353E, L358S, L359N, G360A),construct 8 (F348D, M350D, I353E, L358S, L359N, G360A) Mutation：construct 8 (F348D, M350D, I353E, L358S, L359N, G360A),construct 8 (F348D, M350D, I353E, L358S, L359N, G360A) ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；291 K；20% (w/v) PAA 5100 Na, 100 mM Hepes pH 8.0, 2.5% (v/v) glycerol
Resolution 3.60 Å R-free 0.253
5OHP Crystal structure of USP30 (C77A) in complex with Lys6-linked diubiquitin Deposited 2017-07-17 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 64–178（115 aa） Fragment：UNP residues 64-178,UNP residues 217-357,UNP residues 432-502
Chain A 217–357（141 aa） Fragment：UNP residues 64-178,UNP residues 217-357,UNP residues 432-502
Chain A 432–502（71 aa） Fragment：UNP residues 64-178,UNP residues 217-357,UNP residues 432-502
Mutation：construct 13i (C77A, R179G, Q180S, P181G, R182S, F348D, M350S, I353E, L358S, L359N, G360A) Mutation：construct 13i (C77A, R179G, Q180S, P181G, R182S, F348D, M350S, I353E, L358S, L359N, G360A) Mutation：construct 13i (C77A, R179G, Q180S, P181G, R182S, F348D, M350S, I353E, L358S, L359N, G360A) ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；0.73 M sodium citrate, 0.1 M Hepes pH 7.0
Resolution 2.80 Å R-free 0.249
8D0A Crystal structure of human USP30 in complex with a covalent inhibitor 829 and a Fab Deposited 2022-05-25 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 64–178（115 aa）
Chain A 217–357（141 aa）
Chain A 432–502（71 aa）
Mutation：F348D,M350S,I353E Mutation：F348D,M350S,I353E Mutation：F348D,M350S,I353E PKH ~{N}-[(1~{R},2~{R},4~{S},7~{E})-7-[azanyl(sulfanyl)methylidene]-7$l^{4}-azabicyclo[2.2.1]heptan-2-yl]-2-chloranyl-4-(6-cyclopropylpyrazin-2-yl)benzamide × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.1 M Tris pH 8.5, 22% PEG 4000, 4% 2,2,2-Trifluoroethanol
Resolution 3.19 Å R-free 0.290
8D1T Crystal structure of human USP30 in complex with a covalent inhibitor 552 and a Fab Deposited 2022-05-27 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 64–178（115 aa）
Chain A 217–357（141 aa）
Chain A 432–502（71 aa）
Mutation：F348D,M350S,I353E Mutation：F348D,M350S,I353E Mutation：F348D,M350S,I353E PXW (1R,2R,4S,7E)-7-[amino(sulfanyl)methylidene]-2-{[(1P)-3-chloro-3'-(1-cyanocyclopropyl)[1,1'-biphenyl]-4-carbonyl]amino}-7-azabicyclo[2.2.1]heptan-7-ium × 1 ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.1 M Tris pH 8.5, 22% PEG 4000, 4% 1,3-Butanediol
Resolution 2.94 Å R-free 0.294
9F19 Human USP30 chimera in complex with NK036 inhibitor Deposited 2024-04-18 Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 64–178（115 aa）
Chain A 217–224（8 aa）
Chain A 249–275（27 aa）
Chain A 318–348（31 aa）
Chain A 437–502（66 aa）
Chain B 64–178（115 aa）
Chain B 217–224（8 aa）
Chain B 249–275（27 aa）
Chain B 318–348（31 aa）
Chain B 437–502（66 aa）
Not recorded A1H8X 4-fluoranyl-~{N}-[(2~{S})-1-[[4-[(2-methyl-1-oxidanyl-propan-2-yl)sulfamoyl]phenyl]amino]-1-oxidanylidene-3-phenyl-propan-2-yl]benzamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；76 mM NaOH, 100 mM Bicine, 10.2% (w/v) PEG 20,000, 1% (v/v) Dioxane, 10 mM L-Proline (Crystal 1)
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；85 mM NaOH, 100 mM Bicine, 10.2% (w/v) PEG 20,000, 1% (v/v) Dioxane, 10 mM L-Proline (Crystal 2)
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；88 mM NaOH, 100 mM Bicine, 11% (w/v) PEG 20,000, 1% (v/v) Dioxane, 10 mM Sarcosine (Crystal 3)
Resolution 2.75 Å R-free 0.266
9F6G Human USP30 chimera bound to Ubiquitin-PA Deposited 2024-05-01 Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 64–178（115 aa）
Chain A 217–224（8 aa）
Chain A 249–275（27 aa）
Chain A 318–348（31 aa）
Chain A 437–502（66 aa）
Not recorded AYE prop-2-en-1-amine × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；0.56 M sodium citrate pH 7.0
Resolution 1.50 Å R-free 0.211
9LYF Structure-based Discovery of Novel non-Covalent Small Molecule Inhibitors of USP30 Deposited 2025-02-20 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 64–178（115 aa）
Chain A 217–357（141 aa）
Chain A 432–502（71 aa）
Mutation：F348D,M350S,I353E Mutation：F348D,M350S,I353E Mutation：F348D,M350S,I353E A1L7W 5-(3-cyanophenyl)-~{N}-[[(3~{S})-1-(iminomethyl)pyrrolidin-3-yl]methyl]-1,3,4-oxadiazole-2-carboxamide × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293.15 K；0.2M Ammonium citrate tribasic pH 7.0, 20% w/v Polyethylene glycol 3350
Resolution 2.58 Å R-free 0.272

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.