8dn5

Cryo-EM structure of human Glycine Receptor alpha1-beta heteromer, glycine-bound state1(open state)

Method: ELECTRON MICROSCOPY Dmax: 128.8 Å Quality: GOOD

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

Glycine receptor subunit alpha-1

Homo sapiens

UniProt P23415

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 Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 29–457 Chain B; UniProt 29–457 Chain C; UniProt 29–457 Chain D; UniProt 29–457 Not recorded Glycine receptor subunit beta,Green fluorescent protein,Glycine receptor beta × 1 (P48167,P42212,A0A2K6CAQ3) GLY GLYCINE × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 DD9 nonane × 4 HP6 HEPTANE × 6 HEX HEXANE × 13 UND UNDECANE × 6 NBU N-BUTANE × 8 D10 DECANE × 3 OCT N-OCTANE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.63 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GLRA1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–367; UniProt 29–457 Author chain B; PDBConstruct 1–367; UniProt 29–457 Author chain C; PDBConstruct 1–367; UniProt 29–457 Author chain D; PDBConstruct 1–367; UniProt 29–457

Glycine receptor subunit beta,Green fluorescent protein,Glycine receptor beta

Homo sapiens

UniProt A0A2K6CAQ3

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 Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 379–480 Not recorded Glycine receptor subunit alpha-1 × 4 (P23415) GLY GLYCINE × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 DD9 nonane × 4 HP6 HEPTANE × 6 HEX HEXANE × 13 UND UNDECANE × 6 NBU N-BUTANE × 8 D10 DECANE × 3 OCT N-OCTANE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.63 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A2K6CAQ3_MACNE
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 579–680; UniProt 379–480

Glycine receptor subunit beta,Green fluorescent protein,Glycine receptor beta

Homo sapiens

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 Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 1–238 Not recorded Glycine receptor subunit alpha-1 × 4 (P23415) GLY GLYCINE × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 DD9 nonane × 4 HP6 HEPTANE × 6 HEX HEXANE × 13 UND UNDECANE × 6 NBU N-BUTANE × 8 D10 DECANE × 3 OCT N-OCTANE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.63 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 2
Chains and sequence ranges Author chain E; PDBConstruct 339–576; UniProt 1–238

Glycine receptor subunit beta,Green fluorescent protein,Glycine receptor beta

Homo sapiens

UniProt P48167

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 Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 25–355 Not recorded Glycine receptor subunit alpha-1 × 4 (P23415) GLY GLYCINE × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 DD9 nonane × 4 HP6 HEPTANE × 6 HEX HEXANE × 13 UND UNDECANE × 6 NBU N-BUTANE × 8 D10 DECANE × 3 OCT N-OCTANE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.63 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.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GLRB_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–331; UniProt 25–355

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 8dn5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8dn5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8dn5
Deposition date deposition_date2022-07-10
Structure title titleCryo-EM structure of human Glycine Receptor alpha1-beta heteromer, glycine-bound state1(open state)
Keywords keywordsglycine receptor subunit alpha-1, glycine receptor subunit beta, Green fluorescent protein, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.27
Radius of gyration Rg (electron density) rg_electron38.90
Forward intensity I(0) i0504183000.00
Molecular weight molecular_weight200080.0 kDa
Excluded volume excluded_volume257410 ų
Envelope volume envelope_volume338860 ų
Hydration-shell volume shell_volume70915 ų
Envelope diameter envelope_diameter131.9
Shell Rg shell_rg46.21
Envelope Rg envelope_rg38.32
Shape Rg shape_rg38.89
Total Rg total_rg39.38
Total atoms total_atoms14765
Residues n_residues1684
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 dmax128.8
Rg (real space) rg_real39.19
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real5.0420e+08
I(0) uncertainty (real space) i0_real_error8.0230e+06
Rg (reciprocal space) rg_reciprocal39.24
I(0) (reciprocal space) i0_reciprocal504200000.0000
Solution quality estimate total_estimate0.8740
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.3
Skewness Skewness skewness0.340
Kurtosis Kurtosis kurtosis-0.274
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha77140000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.828; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.878

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)