9gry

Cryo-EM structure of human SLC35B1-Q113F variant with AMP-PNP

Method: ELECTRON MICROSCOPY Dmax: 104.1 Å Quality: GOOD

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

Maltodextrin-binding protein

Mus musculus

UniProt A0A4P1LXE0

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 2–370 Not recorded human SLC35B1-Q113F × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

28 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A4P1LXE0_SERSF
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 114–482; UniProt 2–370

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 9gry

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9gry
Deposition date deposition_date2024-09-13
Structure title titleCryo-EM structure of human SLC35B1-Q113F variant with AMP-PNP
Keywords keywordsATP:ADP exchanger, AXER, AMP-PNP, 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_guinier28.90
Radius of gyration Rg (electron density) rg_electron28.88
Forward intensity I(0) i053729100.00
Molecular weight molecular_weight60395.0 kDa
Excluded volume excluded_volume76809 ų
Envelope volume envelope_volume96246 ų
Hydration-shell volume shell_volume28807 ų
Envelope diameter envelope_diameter113.2
Shell Rg shell_rg34.65
Envelope Rg envelope_rg29.49
Shape Rg shape_rg28.88
Total Rg total_rg29.48
Total atoms total_atoms8482
Residues n_residues536
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 dmax104.1
Rg (real space) rg_real29.08
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real5.3730e+07
I(0) uncertainty (real space) i0_real_error7.7110e+05
Rg (reciprocal space) rg_reciprocal29.01
I(0) (reciprocal space) i0_reciprocal53730000.0000
Solution quality estimate total_estimate0.8140
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.5
Skewness Skewness skewness0.508
Kurtosis Kurtosis kurtosis-0.295
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11770000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.673; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.611; Smooth: 0.947

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)