9hpc

The TMD and the LBD region of the AMPAR complex GluA3- TARP gamma2 in the apo state.

Method: ELECTRON MICROSCOPY Dmax: 143.7 Å Quality: GOOD

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

Isoform Flip of Glutamate receptor 3,Voltage-dependent calcium channel gamma-2 subunit

Rattus norvegicus

UniProt P19492

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 Homooligomer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 24–865 Chain B; UniProt 24–865 Chain C; UniProt 24–865 Chain D; UniProt 24–865 Chain W; UniProt 24–865 Chain X; UniProt 24–865 Chain Y; UniProt 24–865 Chain Z; UniProt 24–865 Mutation:R439G No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.59 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.

32 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIA3_RAT
Isoform P19492-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 10–851; UniProt 24–865 Author chain B; PDBConstruct 10–851; UniProt 24–865 Author chain C; PDBConstruct 10–851; UniProt 24–865 Author chain D; PDBConstruct 10–851; UniProt 24–865 Author chain W; PDBConstruct 10–851; UniProt 24–865 Author chain X; PDBConstruct 10–851; UniProt 24–865 Author chain Y; PDBConstruct 10–851; UniProt 24–865 Author chain Z; PDBConstruct 10–851; UniProt 24–865

Isoform Flip of Glutamate receptor 3,Voltage-dependent calcium channel gamma-2 subunit

Rattus norvegicus

UniProt Q71RJ2

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 Homooligomer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 2–323 Chain B; UniProt 2–323 Chain C; UniProt 2–323 Chain D; UniProt 2–323 Chain W; UniProt 2–323 Chain X; UniProt 2–323 Chain Y; UniProt 2–323 Chain Z; UniProt 2–323 Mutation:R439G No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.59 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.

31 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCG2_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 858–1179; UniProt 2–323 Author chain B; PDBConstruct 858–1179; UniProt 2–323 Author chain C; PDBConstruct 858–1179; UniProt 2–323 Author chain D; PDBConstruct 858–1179; UniProt 2–323 Author chain W; PDBConstruct 858–1179; UniProt 2–323 Author chain X; PDBConstruct 858–1179; UniProt 2–323 Author chain Y; PDBConstruct 858–1179; UniProt 2–323 Author chain Z; PDBConstruct 858–1179; UniProt 2–323

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 9hpc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9hpc
Deposition date deposition_date2024-12-12
Structure title titleThe TMD and the LBD region of the AMPAR complex GluA3- TARP gamma2 in the apo state.
Keywords keywordsAMPAR, ion channels, neurotransmission, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.44
Radius of gyration Rg (electron density) rg_electron44.82
Forward intensity I(0) i0833775000.00
Molecular weight molecular_weight254740.0 kDa
Excluded volume excluded_volume325190 ų
Envelope volume envelope_volume446220 ų
Hydration-shell volume shell_volume81213 ų
Envelope diameter envelope_diameter143.7
Shell Rg shell_rg51.08
Envelope Rg envelope_rg43.71
Shape Rg shape_rg44.82
Total Rg total_rg45.12
Total atoms total_atoms35941
Residues n_residues2307
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 dmax143.7
Rg (real space) rg_real45.23
Rg uncertainty (real space) rg_real_error0.92
I(0) (real space) i0_real8.3380e+08
I(0) uncertainty (real space) i0_real_error1.4330e+07
Rg (reciprocal space) rg_reciprocal45.44
I(0) (reciprocal space) i0_reciprocal834000000.0000
Solution quality estimate total_estimate0.8925
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.5
Skewness Skewness skewness0.156
Kurtosis Kurtosis kurtosis-0.514
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha72200000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.928; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.825

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)