21np

Structure of human SLC37A4 bound to chlorogenic acid in a lipid nanodisc

Method: ELECTRON MICROSCOPY Dmax: 70.8 Å Quality: EXCELLENT

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

Glucose-6-phosphate exchanger SLC37A4

Homo sapiens

UniProt O43826

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 1–429 Not recorded A1EG7 (1S,3R,4R,5R)-3-[(E)-3-[3,4-bis(oxidanyl)phenyl]prop-2-enoyl]oxy-1,4,5-tris(oxidanyl)cyclohexane-1-carboxylic acid × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

24 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G6PT1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–429; UniProt 1–429

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 21np

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 21np
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2. Structure Basics 2. Structure Basics

Entry ID entry_id21np
Deposition date deposition_date2025-12-21
Structure title titleStructure of human SLC37A4 bound to chlorogenic acid in a lipid nanodisc
Keywords keywordstransporter, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier22.48
Radius of gyration Rg (electron density) rg_electron21.70
Forward intensity I(0) i061980400.00
Molecular weight molecular_weight42698.0 kDa
Excluded volume excluded_volume42203 ų
Envelope volume envelope_volume67867 ų
Hydration-shell volume shell_volume25632 ų
Envelope diameter envelope_diameter74.1
Shell Rg shell_rg29.12
Envelope Rg envelope_rg22.06
Shape Rg shape_rg21.72
Total Rg total_rg22.37
Total atoms total_atoms3244
Residues n_residues422
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 dmax70.8
Rg (real space) rg_real22.40
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real6.1980e+07
I(0) uncertainty (real space) i0_real_error8.1570e+05
Rg (reciprocal space) rg_reciprocal22.42
I(0) (reciprocal space) i0_reciprocal61980000.0000
Solution quality estimate total_estimate0.9036
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.8
Skewness Skewness skewness0.250
Kurtosis Kurtosis kurtosis-0.410
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9102000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.918; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)