9j97

Closed structure of human XPR1

Method: ELECTRON MICROSCOPY Dmax: 118.6 Å Quality: GOOD

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

Solute carrier family 53 member 1,Green fluorescent protein

Aequorea victoria

UniProt P42212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–238 Chain B; UniProt 2–238 Not recorded 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CLR CHOLESTEROL × 2 PO4 PHOSPHATE ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 713–949; UniProt 2–238 Author chain B; PDBConstruct 713–949; UniProt 2–238

Solute carrier family 53 member 1,Green fluorescent protein

Aequorea victoria

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 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–696 Chain B; UniProt 1–696 Not recorded 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CLR CHOLESTEROL × 2 PO4 PHOSPHATE ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 9j97

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9j97
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9j97
Deposition date deposition_date2024-08-22
Structure title titleClosed structure of human XPR1
Keywords keywordsXPR1, Phosphate exporter, transporter, membrane protein, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.22
Radius of gyration Rg (electron density) rg_electron35.28
Forward intensity I(0) i0109051000.00
Molecular weight molecular_weight94514.0 kDa
Excluded volume excluded_volume122610 ų
Envelope volume envelope_volume156810 ų
Hydration-shell volume shell_volume38074 ų
Envelope diameter envelope_diameter120.2
Shell Rg shell_rg40.30
Envelope Rg envelope_rg34.79
Shape Rg shape_rg35.28
Total Rg total_rg35.71
Total atoms total_atoms6704
Residues n_residues786
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 dmax118.6
Rg (real space) rg_real36.34
Rg uncertainty (real space) rg_real_error1.23
I(0) (real space) i0_real1.0910e+08
I(0) uncertainty (real space) i0_real_error1.9220e+06
Rg (reciprocal space) rg_reciprocal36.27
I(0) (reciprocal space) i0_reciprocal109000000.0000
Solution quality estimate total_estimate0.8783
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.298
Kurtosis Kurtosis kurtosis-0.702
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8946000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.899; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.876; Smooth: 0.843

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)