9w1o

Phosphate-bound human SLC37A4 antiparallel dimer

Method: ELECTRON MICROSCOPY Dmax: 106.4 Å Quality: GOOD

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 PO4 PHOSPHATE ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 9w1o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9w1o
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9w1o
Deposition date deposition_date2025-07-26
Structure title titlePhosphate-bound human SLC37A4 antiparallel dimer
Keywords keywordsSLC37A4, G6PT, G6P, Phosphate, GSD-Ib, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier32.82
Radius of gyration Rg (electron density) rg_electron32.80
Forward intensity I(0) i0105518000.00
Molecular weight molecular_weight88201.0 kDa
Excluded volume excluded_volume112820 ų
Envelope volume envelope_volume141680 ų
Hydration-shell volume shell_volume36550 ų
Envelope diameter envelope_diameter114.6
Shell Rg shell_rg39.01
Envelope Rg envelope_rg32.47
Shape Rg shape_rg32.82
Total Rg total_rg33.25
Total atoms total_atoms6224
Residues n_residues814
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 dmax106.4
Rg (real space) rg_real32.94
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real1.0550e+08
I(0) uncertainty (real space) i0_real_error1.7890e+06
Rg (reciprocal space) rg_reciprocal32.90
I(0) (reciprocal space) i0_reciprocal105500000.0000
Solution quality estimate total_estimate0.8904
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.2
Skewness Skewness skewness0.352
Kurtosis Kurtosis kurtosis-0.556
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12070000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.922; Smooth: 0.870

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)