9bvh

Homomeric alpha3 glycine receptor in the presence of 0.1 mM glycine in an apo state.

Method: ELECTRON MICROSCOPY Dmax: 132.8 Å Quality: GOOD

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

Glycine receptor subunit alpha-3

Homo sapiens

UniProt O75311

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Homooligomer Protein × 5 其他Polymer 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–464 Chain B; UniProt 1–464 Chain C; UniProt 1–464 Chain D; UniProt 1–464 Chain E; UniProt 1–464 Not recorded 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 20 PX4 1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 20 CLR CHOLESTEROL × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.58 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.

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GLRA3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–464; UniProt 1–464 Author chain B; PDBConstruct 1–464; UniProt 1–464 Author chain C; PDBConstruct 1–464; UniProt 1–464 Author chain D; PDBConstruct 1–464; UniProt 1–464 Author chain E; PDBConstruct 1–464; UniProt 1–464

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 9bvh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9bvh
Deposition date deposition_date2024-05-20
Structure title titleHomomeric alpha3 glycine receptor in the presence of 0.1 mM glycine in an apo state.
Keywords keywordsGlycine, Ion Channel, Ligand-Gated, Pentameric, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.19
Radius of gyration Rg (electron density) rg_electron39.85
Forward intensity I(0) i0541213000.00
Molecular weight molecular_weight208170.0 kDa
Excluded volume excluded_volume267790 ų
Envelope volume envelope_volume353180 ų
Hydration-shell volume shell_volume72075 ų
Envelope diameter envelope_diameter133.6
Shell Rg shell_rg46.82
Envelope Rg envelope_rg39.49
Shape Rg shape_rg39.86
Total Rg total_rg40.21
Total atoms total_atoms14660
Residues n_residues1710
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 dmax132.8
Rg (real space) rg_real40.15
Rg uncertainty (real space) rg_real_error1.01
I(0) (real space) i0_real5.4120e+08
I(0) uncertainty (real space) i0_real_error9.4840e+06
Rg (reciprocal space) rg_reciprocal40.19
I(0) (reciprocal space) i0_reciprocal541200000.0000
Solution quality estimate total_estimate0.8760
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.7
Skewness Skewness skewness0.353
Kurtosis Kurtosis kurtosis-0.305
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha106100000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.827; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.902

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)