9n9y

Crystal structure of truncated USP1:UAF1 in complex with compound 18

Method: X-RAY DIFFRACTION Dmax: 112.2 Å Quality: REASONABLE

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

WD repeat-containing protein 48

Homo sapiens

UniProt Q8TAF3

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–563 Fragment:residues 1-563 Ubiquitin carboxyl-terminal hydrolase 1, N-terminal fragment,Ubiquitin carboxyl-terminal hydrolase 1 × 1 (O94782) ZN ZINC ION × 1 A1BWW 2-(4-cyclopropyl-6-methoxypyrimidin-5-yl)-7-({4-[1-methyl-4-(trifluoromethyl)-1H-imidazol-2-yl]phenyl}methyl)-5H-pyrrolo[3,2-d]pyrimidine × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;1M sodium citrate (pH 6.5) Resolution 3.15 Å R-free 0.291

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.

18 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WDR48_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–563; UniProt 1–563

Ubiquitin carboxyl-terminal hydrolase 1, N-terminal fragment,Ubiquitin carboxyl-terminal hydrolase 1

Homo sapiens

UniProt O94782

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 85–222 Chain B; UniProt 421–605 Chain B; UniProt 739–785 Mutation:residues 1-84 deleted, residues 223-440 replaced with GSGSGSGSGS, residues 606-738 deleted WD repeat-containing protein 48 × 1 (Q8TAF3) ZN ZINC ION × 1 A1BWW 2-(4-cyclopropyl-6-methoxypyrimidin-5-yl)-7-({4-[1-methyl-4-(trifluoromethyl)-1H-imidazol-2-yl]phenyl}methyl)-5H-pyrrolo[3,2-d]pyrimidine × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;1M sodium citrate (pH 6.5) Resolution 3.15 Å R-free 0.291

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.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBP1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–139; UniProt 85–222 Author chain B; PDBConstruct 150–334; UniProt 421–605 Author chain B; PDBConstruct 335–381; UniProt 739–785

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 9n9y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9n9y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9n9y
Deposition date deposition_date2025-02-11
Structure title titleCrystal structure of truncated USP1:UAF1 in complex with compound 18
Keywords keywordsubiquitin, cysteine protease, allosteric inhibitor, HYDROLASE, HYDROLASE-INHIBITOR complex; HYDROLASE/INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.38
Radius of gyration Rg (electron density) rg_electron35.17
Forward intensity I(0) i0276368000.00
Molecular weight molecular_weight89008.0 kDa
Excluded volume excluded_volume85859 ų
Envelope volume envelope_volume162310 ų
Hydration-shell volume shell_volume39005 ų
Envelope diameter envelope_diameter114.8
Shell Rg shell_rg40.92
Envelope Rg envelope_rg34.77
Shape Rg shape_rg35.18
Total Rg total_rg35.48
Total atoms total_atoms6729
Residues n_residues844
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 dmax112.2
Rg (real space) rg_real35.43
Rg uncertainty (real space) rg_real_error0.85
I(0) (real space) i0_real2.7640e+08
I(0) uncertainty (real space) i0_real_error4.7240e+06
Rg (reciprocal space) rg_reciprocal35.40
I(0) (reciprocal space) i0_reciprocal276400000.0000
Solution quality estimate total_estimate0.6865
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.9
Skewness Skewness skewness0.253
Kurtosis Kurtosis kurtosis-0.810
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha45880000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.869; Stabil: 1.000; Sysdev: 0.186; Positv: 1.000; Valcen: 0.930; Smooth: 0.823

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)