9jxg

Cryo-EM structure of apo human XPR1, class 3, with symmetrically dimerized SPX domains

Method: ELECTRON MICROSCOPY Dmax: 118.4 Å Quality: REASONABLE

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

Solute carrier family 53 member 1

Homo sapiens

UniProt Q9UBH6

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 1–696 Chain B; UniProt 1–696 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.75 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.

50 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name S53A1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–696; UniProt 1–696 Author chain B; PDBConstruct 1–696; UniProt 1–696

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 9jxg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9jxg
Deposition date deposition_date2024-10-11
Structure title titleCryo-EM structure of apo human XPR1, class 3, with symmetrically dimerized SPX domains
Keywords keywordsphosphate channel;phosphate exporter;PFBC, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier38.18
Radius of gyration Rg (electron density) rg_electron37.29
Forward intensity I(0) i0245498000.00
Molecular weight molecular_weight136410.0 kDa
Excluded volume excluded_volume174620 ų
Envelope volume envelope_volume241600 ų
Hydration-shell volume shell_volume53784 ų
Envelope diameter envelope_diameter122.0
Shell Rg shell_rg43.81
Envelope Rg envelope_rg36.37
Shape Rg shape_rg37.28
Total Rg total_rg37.81
Total atoms total_atoms9670
Residues n_residues1160
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 dmax118.4
Rg (real space) rg_real37.97
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real2.4550e+08
I(0) uncertainty (real space) i0_real_error4.1850e+06
Rg (reciprocal space) rg_reciprocal38.11
I(0) (reciprocal space) i0_reciprocal245500000.0000
Solution quality estimate total_estimate0.6764
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.2
Skewness Skewness skewness0.088
Kurtosis Kurtosis kurtosis-0.603
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha20580000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.948; Stabil: 1.000; Sysdev: 0.035; Positv: 1.000; Valcen: 0.990; Smooth: 0.850

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)