8wtv

Cryo-EM structure of noradrenaline transporter in complex with noradrenaline

Method: ELECTRON MICROSCOPY Dmax: 88.0 Å Quality: GOOD

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

Sodium-dependent noradrenaline transporter

Homo sapiens

UniProt P23975

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 52–617 Not recorded NA SODIUM ION × 2 CL CHLORIDE ION × 1 E5E Noradrenaline × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

35 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SC6A2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–566; UniProt 52–617

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 8wtv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8wtv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8wtv
Deposition date deposition_date2023-10-19
Structure title titleCryo-EM structure of noradrenaline transporter in complex with noradrenaline
Keywords keywordsprotein structure, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier25.90
Radius of gyration Rg (electron density) rg_electron24.68
Forward intensity I(0) i049369600.00
Molecular weight molecular_weight60952.0 kDa
Excluded volume excluded_volume78757 ų
Envelope volume envelope_volume93060 ų
Hydration-shell volume shell_volume31321 ų
Envelope diameter envelope_diameter90.4
Shell Rg shell_rg32.17
Envelope Rg envelope_rg24.81
Shape Rg shape_rg24.69
Total Rg total_rg25.52
Total atoms total_atoms4322
Residues n_residues536
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 dmax88.0
Rg (real space) rg_real25.92
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real4.9370e+07
I(0) uncertainty (real space) i0_real_error7.1160e+05
Rg (reciprocal space) rg_reciprocal25.91
I(0) (reciprocal space) i0_reciprocal49370000.0000
Solution quality estimate total_estimate0.8700
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary30.3
Skewness Skewness skewness0.438
Kurtosis Kurtosis kurtosis-0.110
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha9158000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.781; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.976

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)