9f19

Human USP30 chimera in complex with NK036 inhibitor

Method: X-RAY DIFFRACTION D_max: 83.6 Å Quality: GOOD

▼

1. Protein Identity and Related Structures Protein Identity & Related Structures

Ubiquitin carboxyl-terminal hydrolase 30,Ubiquitin carboxyl-terminal hydrolase 14,Ubiquitin carboxyl-terminal hydrolase 35

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 248–272 Chain A； UniProt 295–320 Chain B； UniProt 248–272 Chain B； UniProt 295–320	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

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 9F19	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2AYN Structure of USP14, a proteasome-associated deubiquitinating enzyme Deposited 2005-09-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 90–493（404 aa） Chain B 90–493（404 aa） Chain C 90–493（404 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；290 K；MES, ammonium sulfate, PEG monomethyl ether, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 3.20 Å R-free 0.322
2AYO Structure of USP14 bound to ubquitin aldehyde Deposited 2005-09-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 90–493（404 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；290 K；Tris, calsium chloride, PEG1000, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 3.50 Å R-free 0.330
2AYO Structure of USP14 bound to ubquitin aldehyde Deposited 2005-09-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 90–493（404 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；290 K；Tris, calsium chloride, PEG1000, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 3.50 Å R-free 0.330
5GJQ Structure of the human 26S proteasome bound to USP14-UbAl Deposited 2016-07-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 48 PDB declaration: 48-meric	Chain x 1–494（494 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；blot for 2 seconds before plunging	Resolution 4.35 Å
6IIK USP14 catalytic domain with IU1 Deposited 2018-10-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 96–494（399 aa） Chain B 96–494（399 aa）	Not recorded	IU1 1-[1-(4-fluorophenyl)-2,5-dimethyl-1H-pyrrol-3-yl]-2-(pyrrolidin-1-yl)ethan-1-one × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；NH4F. PEG 3350, glycine, Cscl	Resolution 1.97 Å R-free 0.218
6IIL USP14 catalytic domain bind to IU1-47 Deposited 2018-10-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 96–494（399 aa） Fragment：catalytic domain Chain B 96–494（399 aa） Fragment：catalytic domain	Not recorded	A8F 1-[1-(4-chlorophenyl)-2,5-dimethyl-1H-pyrrol-3-yl]-2-(piperidin-1-yl)ethan-1-one × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；PEG 3350, NH4F, glycine, Cscl	Resolution 2.20 Å R-free 0.232
6IIM USP14 catalytic domain with IU1-206 Deposited 2018-10-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 96–494（399 aa） Fragment：catalytic domain Chain B 96–494（399 aa） Fragment：catalytic domain	Not recorded	A8L 1-[1-(4-chlorophenyl)-2,5-dimethyl-1H-pyrrol-3-yl]-2-(4-hydroxypiperidin-1-yl)ethan-1-one × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；PEG 3350, NH4F, Cscl, glycine	Resolution 2.21 Å R-free 0.247
6IIN USP14 catalytic domain with IU1-248 Deposited 2018-10-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 101–485（385 aa） Fragment：catalytic domain Chain B 101–485（385 aa） Fragment：catalytic domain	Not recorded	A8O 4-{3-[(4-hydroxypiperidin-1-yl)acetyl]-2,5-dimethyl-1H-pyrrol-1-yl}benzonitrile × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；PEG 3350, NH4F, Cscl, glycine	Resolution 2.53 Å R-free 0.264
6LVS USP14 catalytic domain mutant C114S Deposited 2020-02-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 92–494（403 aa） Fragment：catalytic domain	Mutation：C114S, deletion of 223-231	GOL GLYCEROL × 3 NA SODIUM ION × 7 FMT FORMIC ACID × 2 BME BETA-MERCAPTOETHANOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295.15 K；0.2M HcooNa, 0.1M BICINE, 20% PEGmme 5000	Resolution 2.73 Å R-free 0.277
6LVS USP14 catalytic domain mutant C114S Deposited 2020-02-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 92–494（403 aa） Fragment：catalytic domain	Mutation：C114S, deletion of 223-231	GOL GLYCEROL × 3 NA SODIUM ION × 8 FMT FORMIC ACID × 7 BME BETA-MERCAPTOETHANOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295.15 K；0.2M HcooNa, 0.1M BICINE, 20% PEGmme 5000	Resolution 2.73 Å R-free 0.277
6LVS USP14 catalytic domain mutant C114S Deposited 2020-02-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 92–494（403 aa） Fragment：catalytic domain	Mutation：C114S, deletion of 223-231	GOL GLYCEROL × 2 NA SODIUM ION × 8 FMT FORMIC ACID × 6 BME BETA-MERCAPTOETHANOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295.15 K；0.2M HcooNa, 0.1M BICINE, 20% PEGmme 5000	Resolution 2.73 Å R-free 0.277
6LVS USP14 catalytic domain mutant C114S Deposited 2020-02-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 92–494（403 aa） Fragment：catalytic domain	Mutation：C114S, deletion of 223-231	GOL GLYCEROL × 2 NA SODIUM ION × 5 FMT FORMIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295.15 K；0.2M HcooNa, 0.1M BICINE, 20% PEGmme 5000	Resolution 2.73 Å R-free 0.277
6LVS USP14 catalytic domain mutant C114S Deposited 2020-02-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain E 92–494（403 aa） Fragment：catalytic domain	Mutation：C114S, deletion of 223-231	GOL GLYCEROL × 2 NA SODIUM ION × 7 FMT FORMIC ACID × 5 BME BETA-MERCAPTOETHANOL × 3 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295.15 K；0.2M HcooNa, 0.1M BICINE, 20% PEGmme 5000	Resolution 2.73 Å R-free 0.277
6LVS USP14 catalytic domain mutant C114S Deposited 2020-02-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain F 92–494（403 aa） Fragment：catalytic domain	Mutation：C114S, deletion of 223-231	NA SODIUM ION × 6 FMT FORMIC ACID × 4 BME BETA-MERCAPTOETHANOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295.15 K；0.2M HcooNa, 0.1M BICINE, 20% PEGmme 5000	Resolution 2.73 Å R-free 0.277
7W37 Structure of USP14-bound human 26S proteasome in state EA1_UBL Deposited 2021-11-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 47 PDB declaration: 47-meric	Chain x 1–494（494 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 6 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
7W38 Structure of USP14-bound human 26S proteasome in state EA2.0_UBL Deposited 2021-11-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 48 PDB declaration: 48-meric	Chain x 1–494（494 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 6 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
7W39 Structure of USP14-bound human 26S proteasome in state EA2.1_UBL Deposited 2021-11-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 49 PDB declaration: 49-meric	Chain x 1–494（494 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
7W3A Structure of USP14-bound human 26S proteasome in substrate-engaged state ED4_USP14 Deposited 2021-11-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 49 PDB declaration: 49-meric	Chain x 1–494（494 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
7W3B Structure of USP14-bound human 26S proteasome in substrate-engaged state ED5_USP14 Deposited 2021-11-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 49 PDB declaration: 49-meric	Chain x 1–494（494 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
7W3C Structure of USP14-bound human 26S proteasome in substrate-engaged state ED0_USP14 Deposited 2021-11-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 49 PDB declaration: 49-meric	Chain x 1–494（494 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
7W3F Structure of USP14-bound human 26S proteasome in substrate-engaged state ED1_USP14 Deposited 2021-11-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 49 PDB declaration: 49-meric	Chain x 1–494（494 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
7W3G Structure of USP14-bound human 26S proteasome in substrate-engaged state ED2.0_USP14 Deposited 2021-11-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 49 PDB declaration: 49-meric	Chain x 1–494（494 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
7W3H Structure of USP14-bound human 26S proteasome in substrate-engaged state ED2.1_USP14 Deposited 2021-11-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 49 PDB declaration: 49-meric	Chain x 1–494（494 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
7W3I Structure of USP14-bound human 26S proteasome in substrate-inhibited state SB_USP14 Deposited 2021-11-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 48 PDB declaration: 48-meric	Chain x 1–494（494 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
7W3J Structure of USP14-bound human 26S proteasome in substrate-inhibited state SC_USP14 Deposited 2021-11-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 48 PDB declaration: 48-meric	Chain x 1–494（494 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.50 Å
7W3K Structure of USP14-bound human 26S proteasome in substrate-inhibited state SD4_USP14 Deposited 2021-11-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 48 PDB declaration: 48-meric	Chain x 1–494（494 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
7W3M Structure of USP14-bound human 26S proteasome in substrate-inhibited state SD5_USP14 Deposited 2021-11-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 48 PDB declaration: 48-meric	Chain x 1–494（494 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
9F6G Human USP30 chimera bound to Ubiquitin-PA Deposited 2024-05-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 248–272（25 aa） Chain A 295–320（26 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

22 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	UBP14_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 130–154； UniProt 248–272 Author chain A； PDBConstruct 182–207； UniProt 295–320 Author chain B； PDBConstruct 130–154； UniProt 248–272 Author chain B； PDBConstruct 182–207； UniProt 295–320

Ubiquitin carboxyl-terminal hydrolase 30,Ubiquitin carboxyl-terminal hydrolase 14,Ubiquitin carboxyl-terminal hydrolase 35

Homo sapiens

UniProt Q70CQ3

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 64–178 Chain A； UniProt 217–224 Chain A； UniProt 249–275 Chain A； UniProt 318–348 Chain A； UniProt 437–502 Chain B； UniProt 64–178 Chain B； UniProt 217–224 Chain B； UniProt 249–275 Chain B； UniProt 318–348 Chain B； UniProt 437–502	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

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 9F19	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5OHK Crystal structure of USP30 in covalent complex with ubiquitin propargylamide (high resolution) Deposited 2017-07-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	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
9F6G Human USP30 chimera bound to Ubiquitin-PA Deposited 2024-05-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	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	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	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

7 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	UBP30_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–117； UniProt 64–178 Author chain A； PDBConstruct 122–129； UniProt 217–224 Author chain A； PDBConstruct 155–181； UniProt 249–275 Author chain A； PDBConstruct 208–238； UniProt 318–348 Author chain A； PDBConstruct 252–317； UniProt 437–502 Author chain B； PDBConstruct 3–117； UniProt 64–178 Author chain B； PDBConstruct 122–129； UniProt 217–224 Author chain B； PDBConstruct 155–181； UniProt 249–275 Author chain B； PDBConstruct 208–238； UniProt 318–348 Author chain B； PDBConstruct 252–317； UniProt 437–502

Ubiquitin carboxyl-terminal hydrolase 30,Ubiquitin carboxyl-terminal hydrolase 14,Ubiquitin carboxyl-terminal hydrolase 35

Homo sapiens

UniProt Q9P2H5

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 833–845 Chain B； UniProt 833–845	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

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 9F19	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5TXK CRYSTAL STRUCTURE OF USP35 C450S IN COMPLEX WITH UBIQUITIN Deposited 2016-11-17	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 423–603（181 aa） Fragment：UNP residues 432-603,UNP residues 754-944 Chain A 754–944（191 aa） Fragment：UNP residues 432-603,UNP residues 754-944	Not recorded	SO4 SULFATE ION × 3 EDO 1,2-ETHANEDIOL × 3 ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；296 K；0.95 M ammonium sulphate 0.1 M HEPES	Resolution 1.84 Å R-free 0.183
7Q44 Crystal structure of RCC1-Like domain 2 of ubiquitin ligase HERC2 in complex with DXDKDED motif of deubiquitinase USP35 Deposited 2021-10-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 988–1002（15 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293.15 K；20% PEG 3350 0.18M tris amonium citrate	Resolution 2.20 Å R-free 0.231
7Q44 Crystal structure of RCC1-Like domain 2 of ubiquitin ligase HERC2 in complex with DXDKDED motif of deubiquitinase USP35 Deposited 2021-10-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 988–1002（15 aa）	Not recorded	CIT CITRIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293.15 K；20% PEG 3350 0.18M tris amonium citrate	Resolution 2.20 Å R-free 0.231
7Q44 Crystal structure of RCC1-Like domain 2 of ubiquitin ligase HERC2 in complex with DXDKDED motif of deubiquitinase USP35 Deposited 2021-10-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 988–1002（15 aa）	Not recorded	CIT CITRIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293.15 K；20% PEG 3350 0.18M tris amonium citrate	Resolution 2.20 Å R-free 0.231
9F6G Human USP30 chimera bound to Ubiquitin-PA Deposited 2024-05-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 833–845（13 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

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	UBP35_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 239–251； UniProt 833–845 Author chain B； PDBConstruct 239–251； UniProt 833–845

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	9f19
Deposition date deposition_date	2024-04-18
Structure title title	Human USP30 chimera in complex with NK036 inhibitor
Keywords keywords	;USP30, Ubiquitin, inhibitor, DUB, deubiquitinating enzyme, USP14, USP35, mitophagy, USP, Ubiquitin-specific protease, Ubiquitin carboxyl-terminal hydrolase 30, Compound 39, Sulfonamide, Phenylalanine, HYDROLASE ;; HYDROLASE
Experimental Method method	X-RAY DIFFRACTION

▼

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	25.90 Å
Radius of gyration Rg (electron density) rg_electron	25.23 Å
Forward intensity I(0) i0	93457500.00
Molecular weight molecular_weight	50961.0 kDa
Excluded volume excluded_volume	49431 Å³
Envelope volume envelope_volume	85925 Å³
Hydration-shell volume shell_volume	28711 Å³
Envelope diameter envelope_diameter	85.2 Å
Shell Rg shell_rg	32.21 Å
Envelope Rg envelope_rg	25.08 Å
Shape Rg shape_rg	25.21 Å
Total Rg total_rg	25.83 Å
Total atoms total_atoms	3863
Residues n_residues	503
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	83.6 Å
Rg (real space) rg_real	25.91 Å
Rg uncertainty (real space) rg_real_error	0.59 Å
I(0) (real space) i0_real	9.3460e+07
I(0) uncertainty (real space) i0_real_error	1.4630e+06
Rg (reciprocal space) rg_reciprocal	25.91 Å
I(0) (reciprocal space) i0_reciprocal	93460000.0000
Solution quality estimate total_estimate	0.8915
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	28.8 Å
Skewness Skewness skewness	0.373
Kurtosis Kurtosis kurtosis	-0.380
Angular range angular_range	— – 0.3050 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	15240000.0000
Real-space data points n_real_points	62
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.889; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.927

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Ubiquitin carboxyl-terminal hydrolase 30,Ubiquitin carboxyl-terminal hydrolase 14,Ubiquitin carboxyl-terminal hydrolase 35
Molecular weight formula_weight	36126.7 kDa
EC 编号 ec_number	3.4.19.12
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3932

GPKGLVPGLVNLGNTCFMNSLLQGLSACPAFIRWLEEFTSQYSRDQKEPPSHQYLSLTLLHLLKALSCQEVTDDEVLDASCLLDVLRMYRWQISSFEEQDAHELFHVITSSLEDERDGSGSHWKSQHPFGVEFETTMKCTESEEEEVTKGKENQDSLSLSIPAATWGHPLTLDHCLHHFISQEEITKQSPTLQRNALYIKSSKISRLPQCLCIHLQRLSWSSHGTPLKRHEHVQFNEDLRLPLAGGRGQAYRLMAVVVHHGDMHSGHFVTYRRSPPSARNPLSTSNQWLWVSDDTVRKASLQEVLSSSAYLLFYERV

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	;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 ;
Molecular weight formula_weight	513.6 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	69

▶

8. Citations (1)

▶

Unit-cell length a length_a	55.833 Å
Unit-cell length b length_b	73.835 Å
Unit-cell length c length_c	201.053 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 21 2 21
Space-group number int_tables_number	18
Crystal system crystal_system	orthorhombic

Resolution resolution	2.750 Å
Low-resolution limit resolution_low	59.510 Å
R factor r_factor	0.2229
R_work r_work	0.2181
R_free r_free	0.2661

fit	/app/data/saxs_computation/f1/9f19/9f19.fit
pddf	/app/data/pr_computation/f1/9f19/9f19.pr.out
profile	/app/data/saxs_computation/f1/9f19/9f19.dat

Human USP30 chimera in complex with NK036 inhibitor

1. Protein Identity and Related Structures Protein Identity & Related Structures

Ubiquitin carboxyl-terminal hydrolase 30,Ubiquitin carboxyl-terminal hydrolase 14,Ubiquitin carboxyl-terminal hydrolase 35

State in the Current Structure

Other States of the Same Protein in the Database

Ubiquitin carboxyl-terminal hydrolase 30,Ubiquitin carboxyl-terminal hydrolase 14,Ubiquitin carboxyl-terminal hydrolase 35

State in the Current Structure

Other States of the Same Protein in the Database

Ubiquitin carboxyl-terminal hydrolase 30,Ubiquitin carboxyl-terminal hydrolase 14,Ubiquitin carboxyl-terminal hydrolase 35

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)