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9zfl

Structure of an Engineered Sodium/Iodide Symporter (PF-NIS)

Method: ELECTRON MICROSCOPY Dmax: 81.3 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Sodium/iodide cotransporter

Rattus norvegicus

UniProt Q63008

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 1–618 Mutation：N225Q, N485Q, N497Q, L253P, V254F REO PERRHENATE × 1 NA SODIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 2.58 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.

Other PDB Difference from Current Entry 9ZFL Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7UUY Structure of the sodium/iodide symporter (NIS) Deposited 2022-04-29 Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2–618（617 aa）
Mutation：N225Q, N485Q and N497Q 3PH 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
7UUZ Structure of the sodium/iodide symporter (NIS) in complex with perrhenate and sodium Deposited 2022-04-29 Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2–618（617 aa）
Mutation：N225Q, N485Q and N497Q NA SODIUM ION × 1 REO PERRHENATE × 1 3PH 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å
7UV0 Structure of the sodium/iodide symporter (NIS) in complex with iodide and sodium Deposited 2022-04-29 Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2–618（617 aa）
Mutation：N225Q, N485Q and N497Q NA SODIUM ION × 2 IOD IODIDE ION × 1 3PH 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SC5A5_RAT
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–618； UniProt 1–618

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 9zfl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9zfl
Deposition date deposition_date2025-12-01
Structure title titleStructure of an Engineered Sodium/Iodide Symporter (PF-NIS)
Keywords keywordsNIS iodide SLC5A5 perrhenate, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier23.67 Å
Radius of gyration Rg (electron density) rg_electron22.85 Å
Forward intensity I(0) i040922300.00
Molecular weight molecular_weight53973.0 kDa
Excluded volume excluded_volume69396 ų
Envelope volume envelope_volume78591 ų
Hydration-shell volume shell_volume28178 ų
Envelope diameter envelope_diameter83.3 Å
Shell Rg shell_rg30.60 Å
Envelope Rg envelope_rg23.21 Å
Shape Rg shape_rg22.88 Å
Total Rg total_rg23.69 Å
Total atoms total_atoms3785
Residues n_residues506
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax81.3 Å
Rg (real space) rg_real23.61 Å
Rg uncertainty (real space) rg_real_error0.58 Å
I(0) (real space) i0_real4.0920e+07
I(0) uncertainty (real space) i0_real_error6.1930e+05
Rg (reciprocal space) rg_reciprocal23.63 Å
I(0) (reciprocal space) i0_reciprocal40920000.0000
Solution quality estimate total_estimate0.8687
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.9 Å
Skewness Skewness skewness0.324
Kurtosis Kurtosis kurtosis-0.237
Angular range angular_range— – 0.3350 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7115000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.769; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.991
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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8. Citations (1)

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9. Files and Curves (10)