9c7r

Diheteromeric GluN1/GluN2A (M817V) in digitonin complexed with glycine, glutamate, and GNE-4123

Method: ELECTRON MICROSCOPY Dmax: 182.2 Å Quality: GOOD

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

Glutamate receptor ionotropic, NMDA 1, Green fluorescent protein chimera

Rattus norvegicus

UniProt P35439

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 Heteromer Protein × 4 其他Polymer 20 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–847 Chain C; UniProt 1–847 Not recorded Glutamate receptor ionotropic, NMDA 2A, Green fluorescent protein chimera × 2 (Q00959,P42212) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 20 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 15 ELECTRON MICROSCOPY cryo-EM buffer:pH 9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.99 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.

114 other PDB entries and 120 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDZ1_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–847; UniProt 1–847 Author chain C; PDBConstruct 1–847; UniProt 1–847

Glutamate receptor ionotropic, NMDA 1, Green fluorescent protein chimera

Rattus norvegicus

UniProt P42212

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 Heteromer Protein × 4 其他Polymer 20 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 2–238 Chain B; UniProt 2–238 Chain C; UniProt 2–238 Chain D; UniProt 2–238 Not recorded 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 20 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 15 ELECTRON MICROSCOPY cryo-EM buffer:pH 9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.99 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 859–1095; UniProt 2–238 Author chain C; PDBConstruct 859–1095; UniProt 2–238 Author chain B; PDBConstruct 878–1114; UniProt 2–238 Author chain D; PDBConstruct 878–1114; UniProt 2–238

Glutamate receptor ionotropic, NMDA 2A, Green fluorescent protein chimera

Aequorea victoria

UniProt Q00959

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 Heteromer Protein × 4 其他Polymer 20 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–866 Chain D; UniProt 1–866 Not recorded Glutamate receptor ionotropic, NMDA 1, Green fluorescent protein chimera × 2 (P35439,P42212) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 20 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 15 ELECTRON MICROSCOPY cryo-EM buffer:pH 9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.99 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.

59 other PDB entries and 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDE1_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–877; UniProt 1–866 Author chain D; PDBConstruct 1–877; UniProt 1–866

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 9c7r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9c7r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9c7r
Deposition date deposition_date2024-06-11
Structure title titleDiheteromeric GluN1/GluN2A (M817V) in digitonin complexed with glycine, glutamate, and GNE-4123
Keywords keywordsion channel, NMDA, positive allosteric modulator, pre-open pore conformation, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.16
Radius of gyration Rg (electron density) rg_electron53.51
Forward intensity I(0) i01860710000.00
Molecular weight molecular_weight367590.0 kDa
Excluded volume excluded_volume462940 ų
Envelope volume envelope_volume685710 ų
Hydration-shell volume shell_volume107470 ų
Envelope diameter envelope_diameter183.6
Shell Rg shell_rg55.92
Envelope Rg envelope_rg52.81
Shape Rg shape_rg53.53
Total Rg total_rg53.54
Total atoms total_atoms25867
Residues n_residues3173
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 dmax182.2
Rg (real space) rg_real53.13
Rg uncertainty (real space) rg_real_error1.65
I(0) (real space) i0_real1.8610e+09
I(0) uncertainty (real space) i0_real_error3.5220e+07
Rg (reciprocal space) rg_reciprocal53.19
I(0) (reciprocal space) i0_reciprocal1861000000.0000
Solution quality estimate total_estimate0.8649
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary66.8
Skewness Skewness skewness0.329
Kurtosis Kurtosis kurtosis-0.271
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha217300000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.823; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.784

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)