9fcj

USP1 bound to ML323 and ubiquitin conjugated to FANCD2 (ordered subset, focused refinement)

Method: ELECTRON MICROSCOPY Dmax: 79.8 Å Quality: GOOD

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

Polyubiquitin-C

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 77–152 Not recorded Ubiquitin carboxyl-terminal hydrolase 1 × 1 (O94782) ZN ZINC ION × 1 JDA 5-methyl-2-(2-propan-2-ylphenyl)-~{N}-[[4-(1,2,3-triazol-1-yl)phenyl]methyl]pyrimidin-4-amine × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blotting for 3.0 seconds 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 1
Chains and sequence ranges Author chain C; PDBConstruct 5–80; UniProt 77–152

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 D; UniProt 1–785 Mutation:C90S Polyubiquitin-C × 1 (P0CG48) ZN ZINC ION × 1 JDA 5-methyl-2-(2-propan-2-ylphenyl)-~{N}-[[4-(1,2,3-triazol-1-yl)phenyl]methyl]pyrimidin-4-amine × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;blotting for 3.0 seconds 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 D; PDBConstruct 2–786; UniProt 1–785

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 9fcj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9fcj
Deposition date deposition_date2024-05-15
Structure title titleUSP1 bound to ML323 and ubiquitin conjugated to FANCD2 (ordered subset, focused refinement)
Keywords keywordsINHIBITOR, DEUBIQUITINASE, COMPLEX, ENZYME-SUBSTRATE, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier23.29
Radius of gyration Rg (electron density) rg_electron21.93
Forward intensity I(0) i032146500.00
Molecular weight molecular_weight44747.0 kDa
Excluded volume excluded_volume56567 ų
Envelope volume envelope_volume66448 ų
Hydration-shell volume shell_volume25302 ų
Envelope diameter envelope_diameter82.4
Shell Rg shell_rg29.01
Envelope Rg envelope_rg22.19
Shape Rg shape_rg21.89
Total Rg total_rg22.95
Total atoms total_atoms3145
Residues n_residues389
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 dmax79.8
Rg (real space) rg_real23.26
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real3.2150e+07
I(0) uncertainty (real space) i0_real_error4.5450e+05
Rg (reciprocal space) rg_reciprocal23.27
I(0) (reciprocal space) i0_reciprocal32150000.0000
Solution quality estimate total_estimate0.7845
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary29.5
Skewness Skewness skewness0.387
Kurtosis Kurtosis kurtosis-0.048
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7142000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.735; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)