9wt2

Cryo-EM structure of Pi-free G6PT1 treated with GlcN6P

Method: ELECTRON MICROSCOPY Dmax: 91.5 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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–429 Chain B; UniProt 1–429 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.12 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 Author chain B; 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 9wt2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9wt2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9wt2
Deposition date deposition_date2025-09-15
Structure title titleCryo-EM structure of Pi-free G6PT1 treated with GlcN6P
Keywords keywordsG6P, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier29.80
Radius of gyration Rg (electron density) rg_electron28.85
Forward intensity I(0) i0111238000.00
Molecular weight molecular_weight89557.0 kDa
Excluded volume excluded_volume114570 ų
Envelope volume envelope_volume137990 ų
Hydration-shell volume shell_volume38741 ų
Envelope diameter envelope_diameter98.2
Shell Rg shell_rg36.99
Envelope Rg envelope_rg28.84
Shape Rg shape_rg28.83
Total Rg total_rg29.72
Total atoms total_atoms6320
Residues n_residues828
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 dmax91.5
Rg (real space) rg_real29.65
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real1.1120e+08
I(0) uncertainty (real space) i0_real_error1.5730e+06
Rg (reciprocal space) rg_reciprocal29.72
I(0) (reciprocal space) i0_reciprocal111200000.0000
Solution quality estimate total_estimate0.9109
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.7
Skewness Skewness skewness0.121
Kurtosis Kurtosis kurtosis-0.537
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16810000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.981

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)