9j8b

Human Glycine Transporter 1 in the Apo State with an Inward-Facing Conformation

Method: ELECTRON MICROSCOPY Dmax: 84.7 Å Quality: GOOD

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

Isoform GlyT-1B of Sodium- and chloride-dependent glycine transporter 1

Homo sapiens

UniProt P48067

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 A; UniProt 1–652 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SC6A9_HUMAN
Isoform P48067-3
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–652; UniProt 1–652

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 9j8b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9j8b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9j8b
Deposition date deposition_date2024-08-21
Structure title titleHuman Glycine Transporter 1 in the Apo State with an Inward-Facing Conformation
Keywords keywordshuman glycine transporter 1, GlyT1, apo, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier25.87
Radius of gyration Rg (electron density) rg_electron24.64
Forward intensity I(0) i048451400.00
Molecular weight molecular_weight58869.0 kDa
Excluded volume excluded_volume75635 ų
Envelope volume envelope_volume93508 ų
Hydration-shell volume shell_volume31315 ų
Envelope diameter envelope_diameter86.5
Shell Rg shell_rg32.35
Envelope Rg envelope_rg24.77
Shape Rg shape_rg24.65
Total Rg total_rg25.59
Total atoms total_atoms4158
Residues n_residues524
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 dmax84.7
Rg (real space) rg_real25.85
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real4.8450e+07
I(0) uncertainty (real space) i0_real_error6.8490e+05
Rg (reciprocal space) rg_reciprocal25.86
I(0) (reciprocal space) i0_reciprocal48450000.0000
Solution quality estimate total_estimate0.8848
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.6
Skewness Skewness skewness0.379
Kurtosis Kurtosis kurtosis-0.213
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9204000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.847; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.958

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)