9di1

Cryo-EM structure of the USP1-UAF1-Ubiquitin complex inhibited by KSQ-4279

Method: ELECTRON MICROSCOPY Dmax: 112.8 Å Quality: EXCELLENT

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–677 Not recorded Ubiquitin carboxyl-terminal hydrolase 1 × 1 (O94782) Ubiquitin × 1 (P0CG48) ZN ZINC ION × 1 A1IB8 6-(4-cyclopropyl-6-methoxy-pyrimidin-5-yl)-1-[[4-[1-propan-2-yl-4-(trifluoromethyl)imidazol-2-yl]phenyl]methyl]pyrazolo[3,4-d]pyrimidine × 1 A1A4Y 3-(methanesulfonyl)propan-1-amine × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 Å

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 1–677; UniProt 1–677

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–785 Not recorded WD repeat-containing protein 48 × 1 (Q8TAF3) Ubiquitin × 1 (P0CG48) ZN ZINC ION × 1 A1IB8 6-(4-cyclopropyl-6-methoxy-pyrimidin-5-yl)-1-[[4-[1-propan-2-yl-4-(trifluoromethyl)imidazol-2-yl]phenyl]methyl]pyrazolo[3,4-d]pyrimidine × 1 A1A4Y 3-(methanesulfonyl)propan-1-amine × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 Å

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 1–785; UniProt 1–785

Ubiquitin

Homo sapiens

UniProt P0CG48

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–75 Not recorded WD repeat-containing protein 48 × 1 (Q8TAF3) Ubiquitin carboxyl-terminal hydrolase 1 × 1 (O94782) ZN ZINC ION × 1 A1IB8 6-(4-cyclopropyl-6-methoxy-pyrimidin-5-yl)-1-[[4-[1-propan-2-yl-4-(trifluoromethyl)imidazol-2-yl]phenyl]methyl]pyrazolo[3,4-d]pyrimidine × 1 A1A4Y 3-(methanesulfonyl)propan-1-amine × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 Å

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.

219 other PDB entries and 348 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBC_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–75; UniProt 1–75

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 9di1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9di1
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9di1
Deposition date deposition_date2024-09-04
Structure title titleCryo-EM structure of the USP1-UAF1-Ubiquitin complex inhibited by KSQ-4279
Keywords keywordsProtease, Thiol-protease, DNA-repair, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.96
Radius of gyration Rg (electron density) rg_electron34.60
Forward intensity I(0) i0394426000.00
Molecular weight molecular_weight106770.0 kDa
Excluded volume excluded_volume103060 ų
Envelope volume envelope_volume187900 ų
Hydration-shell volume shell_volume45247 ų
Envelope diameter envelope_diameter116.2
Shell Rg shell_rg41.13
Envelope Rg envelope_rg34.59
Shape Rg shape_rg34.60
Total Rg total_rg34.93
Total atoms total_atoms8077
Residues n_residues1008
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 dmax112.8
Rg (real space) rg_real34.92
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real3.9440e+08
I(0) uncertainty (real space) i0_real_error6.7530e+06
Rg (reciprocal space) rg_reciprocal34.94
I(0) (reciprocal space) i0_reciprocal394400000.0000
Solution quality estimate total_estimate0.9006
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.1
Skewness Skewness skewness0.231
Kurtosis Kurtosis kurtosis-0.640
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha49360000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.927; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.929

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)