9rxs

Structure of the PDZ4 domain from human PDZK1 (NHERF3) with the C-terminal residues (VLKSTQF) of human URAT1 transporter (SLC22A12)

Method: X-RAY DIFFRACTION Dmax: 53.2 Å Quality: REASONABLE

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

Na(+)/H(+) exchange regulatory cofactor NHE-RF3,Solute carrier family 22 member 12

Homo sapiens

UniProt Q5T2W1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 375–458 Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;100 mM Tris pH 8.5, 100mM NaCl, 18% PEG 10000, 20% Glycerol Resolution 2.00 Å R-free 0.242
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 375–458 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;100 mM Tris pH 8.5, 100mM NaCl, 18% PEG 10000, 20% Glycerol Resolution 2.00 Å R-free 0.242

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.

10 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NHRF3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–85; UniProt 375–458 Author chain B; PDBConstruct 2–85; UniProt 375–458

Na(+)/H(+) exchange regulatory cofactor NHE-RF3,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 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 547–553 Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;100 mM Tris pH 8.5, 100mM NaCl, 18% PEG 10000, 20% Glycerol Resolution 2.00 Å R-free 0.242
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 547–553 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;100 mM Tris pH 8.5, 100mM NaCl, 18% PEG 10000, 20% Glycerol Resolution 2.00 Å R-free 0.242

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 30 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 86–92; UniProt 547–553 Author chain B; PDBConstruct 86–92; UniProt 547–553

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 9rxs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9rxs
Deposition date deposition_date2025-07-11
Structure title titleStructure of the PDZ4 domain from human PDZK1 (NHERF3) with the C-terminal residues (VLKSTQF) of human URAT1 transporter (SLC22A12)
Keywords keywordsScaffold protein, PDZ domain, urate transporter, solute carrier, protein-protein interaction, NHERFs, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.07
Radius of gyration Rg (electron density) rg_electron19.30
Forward intensity I(0) i07217560.00
Molecular weight molecular_weight19858.0 kDa
Excluded volume excluded_volume25114 ų
Envelope volume envelope_volume32945 ų
Hydration-shell volume shell_volume15073 ų
Envelope diameter envelope_diameter82.1
Shell Rg shell_rg24.52
Envelope Rg envelope_rg20.69
Shape Rg shape_rg19.34
Total Rg total_rg20.15
Total atoms total_atoms2839
Residues n_residues183
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 dmax53.2
Rg (real space) rg_real18.88
Rg uncertainty (real space) rg_real_error0.08
I(0) (real space) i0_real6.8570e+06
I(0) uncertainty (real space) i0_real_error6.5920e+04
Rg (reciprocal space) rg_reciprocal20.17
I(0) (reciprocal space) i0_reciprocal7217000.0000
Solution quality estimate total_estimate0.6841
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary20.5
Skewness Skewness skewness0.263
Kurtosis Kurtosis kurtosis-0.494
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha3.7610
Highest regularization parameter α highest_alpha1229000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.002; Oscil: 0.987; Stabil: 0.978; Sysdev: 0.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (2)

9. Files and Curves (10)