9jxk

Cryo-EM structure of human XPR1 in a closed state at the intracellular gate and an open state at the extracellular gate, obtained through local refinement

Method: ELECTRON MICROSCOPY Dmax: 103.9 Å Quality: GOOD

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–625 Not recorded PO4 PHOSPHATE ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.38 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 B; PDBConstruct 1–625; UniProt 1–625

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 9jxk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9jxk
Deposition date deposition_date2024-10-11
Structure title titleCryo-EM structure of human XPR1 in a closed state at the intracellular gate and an open state at the extracellular gate, obtained through local refinement
Keywords keywordsphosphate channel, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier30.87
Radius of gyration Rg (electron density) rg_electron30.21
Forward intensity I(0) i071025800.00
Molecular weight molecular_weight70769.0 kDa
Excluded volume excluded_volume90369 ų
Envelope volume envelope_volume116420 ų
Hydration-shell volume shell_volume33698 ų
Envelope diameter envelope_diameter110.0
Shell Rg shell_rg35.65
Envelope Rg envelope_rg30.36
Shape Rg shape_rg30.18
Total Rg total_rg30.85
Total atoms total_atoms5011
Residues n_residues602
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 dmax103.9
Rg (real space) rg_real31.00
Rg uncertainty (real space) rg_real_error1.03
I(0) (real space) i0_real7.1030e+07
I(0) uncertainty (real space) i0_real_error1.1960e+06
Rg (reciprocal space) rg_reciprocal30.95
I(0) (reciprocal space) i0_reciprocal71020000.0000
Solution quality estimate total_estimate0.8024
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.6
Skewness Skewness skewness0.448
Kurtosis Kurtosis kurtosis-0.288
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8466000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.841; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.907; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)