9fiv

Structure-guided discovery of selective USP7 inhibitors with in vivo activity

Method: X-RAY DIFFRACTION Dmax: 107.5 Å Quality: REASONABLE

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

Ubiquitin carboxyl-terminal hydrolase 7

Homo sapiens

UniProt Q93009

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 207–560 Mutation:F409A A1ICO 7-methyl-3-[[4-oxidanyl-1-[(3~{R},4~{R})-3-phenyl-1-[(5-pyridin-4-yl-1,3-thiazol-2-yl)methyl]piperidin-4-yl]carbonyl-piperidin-4-yl]methyl]pyrrolo[2,3-d]pyrimidin-4-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;292 K;23% peg 3350, 0.6 M sodium formate, 10 mM DTT Resolution 2.70 Å R-free 0.330
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 207–560 Mutation:F409A A1ICO 7-methyl-3-[[4-oxidanyl-1-[(3~{R},4~{R})-3-phenyl-1-[(5-pyridin-4-yl-1,3-thiazol-2-yl)methyl]piperidin-4-yl]carbonyl-piperidin-4-yl]methyl]pyrrolo[2,3-d]pyrimidin-4-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;292 K;23% peg 3350, 0.6 M sodium formate, 10 mM DTT Resolution 2.70 Å R-free 0.330

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.

84 other PDB entries and 144 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBP7_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–355; UniProt 207–560 Author chain B; PDBConstruct 2–355; UniProt 207–560

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

SAXS profile for 9fiv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9fiv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9fiv
Deposition date deposition_date2024-05-29
Structure title titleStructure-guided discovery of selective USP7 inhibitors with in vivo activity
Keywords keywordsHAUSP, USP7, SBDD, HYDROLASE-HYDROLASE INHIBITOR COMPLEX, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.63
Radius of gyration Rg (electron density) rg_electron29.50
Forward intensity I(0) i091987700.00
Molecular weight molecular_weight75342.0 kDa
Excluded volume excluded_volume94086 ų
Envelope volume envelope_volume118950 ų
Hydration-shell volume shell_volume34226 ų
Envelope diameter envelope_diameter110.9
Shell Rg shell_rg35.72
Envelope Rg envelope_rg29.84
Shape Rg shape_rg29.51
Total Rg total_rg30.04
Total atoms total_atoms10488
Residues n_residues650
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax107.5
Rg (real space) rg_real30.67
Rg uncertainty (real space) rg_real_error0.92
I(0) (real space) i0_real9.1990e+07
I(0) uncertainty (real space) i0_real_error1.4390e+06
Rg (reciprocal space) rg_reciprocal30.65
I(0) (reciprocal space) i0_reciprocal91990000.0000
Solution quality estimate total_estimate0.6828
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary33.1
Skewness Skewness skewness0.387
Kurtosis Kurtosis kurtosis-0.229
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16870000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.799; Stabil: 1.000; Sysdev: 0.193; Positv: 1.000; Valcen: 0.925; Smooth: 0.971

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)