SAXSdb — 9f19

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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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Homooligomer	Protein 2	;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 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Homooligomer	Protein 2	;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 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Homooligomer	Protein 2	;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 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

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.

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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

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

9f19__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

9f19__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

9f19__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	26.14 Å
Rg (electron density)	25.20 Å
Total Rg	25.96 Å
Atom count	3863
Residues	503
Excluded volume	67978 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`9f19__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. 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

Source Source

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism 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

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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

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

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

9f19__assembly_1__model_1

9f19__assembly_1__model_1 | I(q)

9f19__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

7. Citations (1)

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

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

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

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

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

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

9f19__assembly_1__model_1

9f19__assembly_1__model_1 | I(q)

9f19__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

7. Citations (1)