7lep

The composite LBD-TMD structure combined from all hippocampal AMPAR subtypes at 3.25 Angstrom resolution

Method: ELECTRON MICROSCOPY Dmax: 148.4 Å Quality: REASONABLE

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

Glutamate receptor 2

OrganismNot specified

UniProt C9K0Z0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 417–840 Chain D; UniProt 417–840 Not recorded Mix of AMPAR subunits (GluA1, GluA3, and GluA4) × 1 Mix of AMPAR subunits (GluA1, GluA3, and GluAX) × 1 Protein cornichon homolog 2 × 2 (O35089) Voltage-dependent calcium channel gamma-8 subunit × 2 (Q8VHW2) ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 30 C14 TETRADECANE × 1 D10 DECANE × 1 XVD 6-[2-chloro-6-(trifluoromethoxy)phenyl]-1H-benzimidazol-2-ol × 2 OCT N-OCTANE × 2 D12 DODECANE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.25 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 C9K0Z0_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–424; UniProt 417–840 Author chain D; PDBConstruct 1–424; UniProt 417–840

Protein cornichon homolog 2

OrganismNot specified

UniProt O35089

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 2–160 Chain F; UniProt 2–160 Not recorded Mix of AMPAR subunits (GluA1, GluA3, and GluA4) × 1 Glutamate receptor 2 × 2 (C9K0Z0) Mix of AMPAR subunits (GluA1, GluA3, and GluAX) × 1 Voltage-dependent calcium channel gamma-8 subunit × 2 (Q8VHW2) ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 30 C14 TETRADECANE × 1 D10 DECANE × 1 XVD 6-[2-chloro-6-(trifluoromethoxy)phenyl]-1H-benzimidazol-2-ol × 2 OCT N-OCTANE × 2 D12 DODECANE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.25 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 CNIH2_MOUSE
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–159; UniProt 2–160 Author chain F; PDBConstruct 1–159; UniProt 2–160

Voltage-dependent calcium channel gamma-8 subunit

OrganismNot specified

UniProt Q8VHW2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain G; UniProt 19–233 Chain H; UniProt 19–233 Not recorded Mix of AMPAR subunits (GluA1, GluA3, and GluA4) × 1 Glutamate receptor 2 × 2 (C9K0Z0) Mix of AMPAR subunits (GluA1, GluA3, and GluAX) × 1 Protein cornichon homolog 2 × 2 (O35089) ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 30 C14 TETRADECANE × 1 D10 DECANE × 1 XVD 6-[2-chloro-6-(trifluoromethoxy)phenyl]-1H-benzimidazol-2-ol × 2 OCT N-OCTANE × 2 D12 DODECANE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.25 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCG8_MOUSE
Isoform
PDB entities 5
Chains and sequence ranges Author chain G; PDBConstruct 1–215; UniProt 19–233 Author chain H; PDBConstruct 1–215; UniProt 19–233

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 7lep

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7lep
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7lep
Deposition date deposition_date2021-01-14
Structure title titleThe composite LBD-TMD structure combined from all hippocampal AMPAR subtypes at 3.25 Angstrom resolution
Keywords keywordsNative hippocampal ion channel, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.79
Radius of gyration Rg (electron density) rg_electron45.12
Forward intensity I(0) i0676607000.00
Molecular weight molecular_weight234760.0 kDa
Excluded volume excluded_volume301530 ų
Envelope volume envelope_volume422790 ų
Hydration-shell volume shell_volume77003 ų
Envelope diameter envelope_diameter154.2
Shell Rg shell_rg50.34
Envelope Rg envelope_rg44.55
Shape Rg shape_rg45.14
Total Rg total_rg45.31
Total atoms total_atoms16558
Residues n_residues2222
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 dmax148.4
Rg (real space) rg_real45.64
Rg uncertainty (real space) rg_real_error1.13
I(0) (real space) i0_real6.7660e+08
I(0) uncertainty (real space) i0_real_error1.2610e+07
Rg (reciprocal space) rg_reciprocal45.78
I(0) (reciprocal space) i0_reciprocal676700000.0000
Solution quality estimate total_estimate0.6800
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.7
Skewness Skewness skewness0.217
Kurtosis Kurtosis kurtosis-0.402
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha71570000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 0.115; Positv: 1.000; Valcen: 0.983; Smooth: 0.771

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id7lepB01
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_id7lepD01
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_id7lepG01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily150
Domain ID domain_id7lepH01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily150

8. Citations (1)

9. Files and Curves (10)