9nr6

The structure of Noelin 1 with cerebellar GluA1/A4-ATD

Method: ELECTRON MICROSCOPY Dmax: 206.3 Å Quality: GOOD

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

Glutamate receptor 1

OrganismNot specified

UniProt P19490

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 Heteromer Protein × 8 其他Polymer 12 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 19–391 Chain C; UniProt 19–391 Not recorded Glutamate receptor 4 × 2 (P19493) 11B8 scFv × 2 Noelin × 2 (Q62609) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CA CALCIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.26 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 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIA1_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–373; UniProt 19–391 Author chain C; PDBConstruct 1–373; UniProt 19–391

Glutamate receptor 4

OrganismNot specified

UniProt P19493

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 Heteromer Protein × 8 其他Polymer 12 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 22–399 Chain D; UniProt 22–399 Not recorded Glutamate receptor 1 × 2 (P19490) 11B8 scFv × 2 Noelin × 2 (Q62609) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CA CALCIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.26 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.

25 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIA4_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–378; UniProt 22–399 Author chain D; PDBConstruct 1–378; UniProt 22–399

Noelin

OrganismNot specified

UniProt Q62609

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 Heteromer Protein × 8 其他Polymer 12 PDB declaration: octameric(8) Consistent with protein copy count Chain G; UniProt 204–480 Chain H; UniProt 204–480 Not recorded Glutamate receptor 1 × 2 (P19490) Glutamate receptor 4 × 2 (P19493) 11B8 scFv × 2 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CA CALCIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.26 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name NOE1_RAT
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 1–277; UniProt 204–480 Author chain H; PDBConstruct 1–277; UniProt 204–480

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 9nr6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9nr6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9nr6
Deposition date deposition_date2025-03-14
Structure title titleThe structure of Noelin 1 with cerebellar GluA1/A4-ATD
Keywords keywordsiGluR, CP-AMPA receptors, Noelin 1, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.22
Radius of gyration Rg (electron density) rg_electron54.10
Forward intensity I(0) i01124530000.00
Molecular weight molecular_weight272420.0 kDa
Excluded volume excluded_volume337290 ų
Envelope volume envelope_volume517490 ų
Hydration-shell volume shell_volume80706 ų
Envelope diameter envelope_diameter221.6
Shell Rg shell_rg55.59
Envelope Rg envelope_rg55.50
Shape Rg shape_rg54.25
Total Rg total_rg53.67
Total atoms total_atoms19239
Residues n_residues2512
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 dmax206.3
Rg (real space) rg_real55.69
Rg uncertainty (real space) rg_real_error2.83
I(0) (real space) i0_real1.1250e+09
I(0) uncertainty (real space) i0_real_error2.4300e+07
Rg (reciprocal space) rg_reciprocal54.83
I(0) (reciprocal space) i0_reciprocal1123000000.0000
Solution quality estimate total_estimate0.8089
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary58.9
Skewness Skewness skewness0.627
Kurtosis Kurtosis kurtosis0.138
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha60220000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.635; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.891; Smooth: 0.718

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)