7qn6

Cryo-EM structure of human full-length beta3delta GABA(A)R in complex with nanobody Nb25

Method: ELECTRON MICROSCOPY Dmax: 122.8 Å Quality: GOOD

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

Gamma-aminobutyric acid receptor subunit beta-3

Homo sapiens

UniProt P28472

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 Heteromer Protein × 8 其他Polymer 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–473 Chain B; UniProt 1–473 Chain C; UniProt 1–473 Chain D; UniProt 1–473 Not recorded Gamma-aminobutyric acid receptor subunit delta × 1 (O14764) Nanobody Nb25 × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 4 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

94 other PDB entries and 94 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBRB3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–473; UniProt 1–473 Author chain B; PDBConstruct 1–473; UniProt 1–473 Author chain C; PDBConstruct 1–473; UniProt 1–473 Author chain D; PDBConstruct 1–473; UniProt 1–473

Gamma-aminobutyric acid receptor subunit delta

Homo sapiens

UniProt O14764

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 Heteromer Protein × 8 其他Polymer 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 1–452 Not recorded Gamma-aminobutyric acid receptor subunit beta-3 × 4 (P28472) Nanobody Nb25 × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 4 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBRD_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–452; UniProt 1–452

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 7qn6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7qn6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7qn6
Deposition date deposition_date2021-12-20
Structure title titleCryo-EM structure of human full-length beta3delta GABA(A)R in complex with nanobody Nb25
Keywords keywordspentameric ligand-gated ion channel, neurotransmitter receptor, GABA receptor, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.61
Radius of gyration Rg (electron density) rg_electron38.98
Forward intensity I(0) i0751213000.00
Molecular weight molecular_weight234930.0 kDa
Excluded volume excluded_volume297680 ų
Envelope volume envelope_volume379540 ų
Hydration-shell volume shell_volume77304 ų
Envelope diameter envelope_diameter134.5
Shell Rg shell_rg47.60
Envelope Rg envelope_rg38.62
Shape Rg shape_rg39.03
Total Rg total_rg39.28
Total atoms total_atoms16571
Residues n_residues1995
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 dmax122.8
Rg (real space) rg_real39.29
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real7.5120e+08
I(0) uncertainty (real space) i0_real_error1.3090e+07
Rg (reciprocal space) rg_reciprocal39.49
I(0) (reciprocal space) i0_reciprocal751400000.0000
Solution quality estimate total_estimate0.8947
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.2
Skewness Skewness skewness0.103
Kurtosis Kurtosis kurtosis-0.479
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha96690000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.904; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.944

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id7qn6K01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7qn6L01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7qn6M01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)