8zto

Cryo-EM structure of the human XPR1

Method: ELECTRON MICROSCOPY Dmax: 116.1 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 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 K9G [(2~{R})-1-hexadecanoyloxy-3-[oxidanyl-[2-(trimethyl-$l^{4}-azanyl)ethoxy]phosphoryl]oxy-propan-2-yl] octadec-9-enoate × 2 PO4 PHOSPHATE ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.55 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 8zto

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8zto
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8zto
Deposition date deposition_date2024-06-07
Structure title titleCryo-EM structure of the human XPR1
Keywords keywordsSLC transporter, XPR1, SLC53A1, structural protein, Pi, exporter; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.96
Radius of gyration Rg (electron density) rg_electron34.11
Forward intensity I(0) i0107672000.00
Molecular weight molecular_weight92908.0 kDa
Excluded volume excluded_volume120220 ų
Envelope volume envelope_volume153540 ų
Hydration-shell volume shell_volume38052 ų
Envelope diameter envelope_diameter115.4
Shell Rg shell_rg39.78
Envelope Rg envelope_rg33.99
Shape Rg shape_rg34.10
Total Rg total_rg34.63
Total atoms total_atoms6590
Residues n_residues778
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 dmax116.1
Rg (real space) rg_real35.05
Rg uncertainty (real space) rg_real_error1.14
I(0) (real space) i0_real1.0770e+08
I(0) uncertainty (real space) i0_real_error1.8680e+06
Rg (reciprocal space) rg_reciprocal34.99
I(0) (reciprocal space) i0_reciprocal107700000.0000
Solution quality estimate total_estimate0.8849
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.5
Skewness Skewness skewness0.308
Kurtosis Kurtosis kurtosis-0.650
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9362000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.895; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.914; Smooth: 0.899

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)