4cof

Crystal structure of a human gamma-aminobutyric acid receptor, the GABA(A)R-beta3 homopentamer

Method: X-RAY DIFFRACTION Dmax: 125.0 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 Homooligomer Protein × 5 其他Polymer 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 26–312 Chain A; UniProt 447–473 Chain B; UniProt 26–312 Chain B; UniProt 447–473 Chain C; UniProt 26–312 Chain C; UniProt 447–473 Chain D; UniProt 26–312 Chain D; UniProt 447–473 Chain E; UniProt 26–312 Chain E; UniProt 447–473 Fragment:RESIDUES 26-312,447-473 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 BEN BENZAMIDINE × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 CL CHLORIDE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;11.5% PEG4000 100 MM SODIUM CHLORIDE, 100 MM LITHIUM SULPHATE, 100 MM N-2-ACETAMIDO-IMINODIACETIC ACID, PH 6.5, 2% (W/V) BENZAMIDINE Resolution 2.97 Å R-free 0.226

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 4–310; UniProt 26–312 Author chain A; PDBConstruct 318–344; UniProt 447–473 Author chain B; PDBConstruct 4–310; UniProt 26–312 Author chain B; PDBConstruct 318–344; UniProt 447–473 Author chain C; PDBConstruct 4–310; UniProt 26–312 Author chain C; PDBConstruct 318–344; UniProt 447–473 Author chain D; PDBConstruct 4–310; UniProt 26–312 Author chain D; PDBConstruct 318–344; UniProt 447–473 Author chain E; PDBConstruct 4–310; UniProt 26–312 Author chain E; PDBConstruct 318–344; UniProt 447–473

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 4cof

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4cof
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4cof
Deposition date deposition_date2014-01-28
Structure title titleCrystal structure of a human gamma-aminobutyric acid receptor, the GABA(A)R-beta3 homopentamer
Keywords keywordsTRANSPORT PROTEIN, MEMBRANE PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.47
Radius of gyration Rg (electron density) rg_electron38.16
Forward intensity I(0) i0519909000.00
Molecular weight molecular_weight198030.0 kDa
Excluded volume excluded_volume252400 ų
Envelope volume envelope_volume319240 ų
Hydration-shell volume shell_volume68170 ų
Envelope diameter envelope_diameter130.1
Shell Rg shell_rg45.52
Envelope Rg envelope_rg37.65
Shape Rg shape_rg38.23
Total Rg total_rg38.32
Total atoms total_atoms13972
Residues n_residues1665
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 dmax125.0
Rg (real space) rg_real38.36
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real5.1990e+08
I(0) uncertainty (real space) i0_real_error8.6890e+06
Rg (reciprocal space) rg_reciprocal38.43
I(0) (reciprocal space) i0_reciprocal519900000.0000
Solution quality estimate total_estimate0.8766
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary45.7
Skewness Skewness skewness0.310
Kurtosis Kurtosis kurtosis-0.293
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha70620000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.841; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.877

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

Domain ID domain_id4cofA01
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology170 — Acetylcholine Binding Protein; Chain: A,
Homologous superfamily homologous superfamily10 — Neurotransmitter-gated ion-channel ligand-binding domain
Domain ID domain_id4cofA02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily390 — Neurotransmitter-gated ion-channel transmembrane domain
Domain ID domain_id4cofB01
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology170 — Acetylcholine Binding Protein; Chain: A,
Homologous superfamily homologous superfamily10 — Neurotransmitter-gated ion-channel ligand-binding domain
Domain ID domain_id4cofB02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily390 — Neurotransmitter-gated ion-channel transmembrane domain
Domain ID domain_id4cofC01
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology170 — Acetylcholine Binding Protein; Chain: A,
Homologous superfamily homologous superfamily10 — Neurotransmitter-gated ion-channel ligand-binding domain
Domain ID domain_id4cofC02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily390 — Neurotransmitter-gated ion-channel transmembrane domain
Domain ID domain_id4cofD01
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology170 — Acetylcholine Binding Protein; Chain: A,
Homologous superfamily homologous superfamily10 — Neurotransmitter-gated ion-channel ligand-binding domain
Domain ID domain_id4cofD02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily390 — Neurotransmitter-gated ion-channel transmembrane domain
Domain ID domain_id4cofE01
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology170 — Acetylcholine Binding Protein; Chain: A,
Homologous superfamily homologous superfamily10 — Neurotransmitter-gated ion-channel ligand-binding domain
Domain ID domain_id4cofE02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily390 — Neurotransmitter-gated ion-channel transmembrane domain

8. Citations (1)

9. Files and Curves (10)