8ss8

Structure of AMPA receptor GluA2 complex with auxiliary subunit TARP gamma-5 bound to competitive antagonist ZK and antiepileptic drug perampanel (closed state)

Method: ELECTRON MICROSCOPY Dmax: 203.2 Å Quality: GOOD

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

Glutamate receptor 2, Voltage-dependent calcium channel gamma-5 subunit chimera

Rattus norvegicus

UniProt P19491

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 25–847 Chain B; UniProt 25–847 Chain C; UniProt 25–847 Chain D; UniProt 25–847 Not recorded 6ZP 2-(6'-oxo-1'-phenyl[1',6'-dihydro[2,3'-bipyridine]]-5'-yl)benzonitrile × 4 ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 14 NA SODIUM ION × 2 CLR CHOLESTEROL × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;vitrification carried out in nitrogen atmosphere Resolution 2.81 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.

333 other PDB entries and 482 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIA2_RAT
Isoform P19491-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–817; UniProt 25–847 Author chain B; PDBConstruct 1–817; UniProt 25–847 Author chain C; PDBConstruct 1–817; UniProt 25–847 Author chain D; PDBConstruct 1–817; UniProt 25–847

Glutamate receptor 2, Voltage-dependent calcium channel gamma-5 subunit chimera

Rattus norvegicus

UniProt Q8VHW8

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 4–207 Chain B; UniProt 4–207 Chain C; UniProt 4–207 Chain D; UniProt 4–207 Not recorded 6ZP 2-(6'-oxo-1'-phenyl[1',6'-dihydro[2,3'-bipyridine]]-5'-yl)benzonitrile × 4 ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 14 NA SODIUM ION × 2 CLR CHOLESTEROL × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;vitrification carried out in nitrogen atmosphere Resolution 2.81 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCG5_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 823–1026; UniProt 4–207 Author chain B; PDBConstruct 823–1026; UniProt 4–207 Author chain C; PDBConstruct 823–1026; UniProt 4–207 Author chain D; PDBConstruct 823–1026; UniProt 4–207

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 8ss8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ss8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ss8
Deposition date deposition_date2023-05-08
Structure title titleStructure of AMPA receptor GluA2 complex with auxiliary subunit TARP gamma-5 bound to competitive antagonist ZK and antiepileptic drug perampanel (closed state)
Keywords keywordsAMPA receptor, neurotransmission, TARP gamma-5, perampanel, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier60.02
Radius of gyration Rg (electron density) rg_electron60.48
Forward intensity I(0) i02090000000.00
Molecular weight molecular_weight404270.0 kDa
Excluded volume excluded_volume514030 ų
Envelope volume envelope_volume745570 ų
Hydration-shell volume shell_volume106500 ų
Envelope diameter envelope_diameter195.5
Shell Rg shell_rg58.91
Envelope Rg envelope_rg58.62
Shape Rg shape_rg60.52
Total Rg total_rg60.29
Total atoms total_atoms28476
Residues n_residues3514
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 dmax203.2
Rg (real space) rg_real60.12
Rg uncertainty (real space) rg_real_error2.11
I(0) (real space) i0_real2.0900e+09
I(0) uncertainty (real space) i0_real_error4.7690e+07
Rg (reciprocal space) rg_reciprocal59.89
I(0) (reciprocal space) i0_reciprocal2089000000.0000
Solution quality estimate total_estimate0.8542
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary70.3
Skewness Skewness skewness0.342
Kurtosis Kurtosis kurtosis-0.437
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha130500000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.887; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.443

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id8ss8A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id8ss8B01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id8ss8C01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id8ss8D01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II

8. Citations (1)

9. Files and Curves (10)