9je1

Human URAT1 bound to dotinurad

Method: ELECTRON MICROSCOPY Dmax: 87.0 Å Quality: REASONABLE

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

Solute carrier family 22 member 12

Homo sapiens

UniProt Q96S37

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 1–553 Not recorded A1AIK dotinurad × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

26 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name S22AC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–553; UniProt 1–553

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 9je1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9je1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9je1
Deposition date deposition_date2024-09-01
Structure title titleHuman URAT1 bound to dotinurad
Keywords keywordsURAT1, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier24.93
Radius of gyration Rg (electron density) rg_electron24.28
Forward intensity I(0) i033172200.00
Molecular weight molecular_weight47264.0 kDa
Excluded volume excluded_volume60368 ų
Envelope volume envelope_volume73892 ų
Hydration-shell volume shell_volume26232 ų
Envelope diameter envelope_diameter89.0
Shell Rg shell_rg30.81
Envelope Rg envelope_rg24.94
Shape Rg shape_rg24.30
Total Rg total_rg25.00
Total atoms total_atoms3320
Residues n_residues435
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 dmax87.0
Rg (real space) rg_real26.15
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real3.3270e+07
I(0) uncertainty (real space) i0_real_error4.2970e+05
Rg (reciprocal space) rg_reciprocal25.07
I(0) (reciprocal space) i0_reciprocal33170000.0000
Solution quality estimate total_estimate0.6413
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary26.2
Skewness Skewness skewness0.607
Kurtosis Kurtosis kurtosis-0.090
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha4.6540
Highest regularization parameter α highest_alpha7129000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.758; Stabil: 0.884; Sysdev: 0.000; Positv: 1.000; Valcen: 0.831; Smooth: 0.620

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (2)

9. Files and Curves (10)