7f56

DNQX-bound GluK2-1xNeto2 complex, with asymmetric LBD

Method: ELECTRON MICROSCOPY Dmax: 223.6 Å Quality: GOOD

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

Glutamate receptor ionotropic, kainate 2

Rattus norvegicus

UniProt P42260

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 × 5 其他Polymer 4 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–908 Chain B; UniProt 1–908 Chain C; UniProt 1–908 Chain D; UniProt 1–908 Mutation:F107L Neuropilin and tolloid-like protein 2 × 1 (C6K2K4) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

91 other PDB entries and 106 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIK2_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–908; UniProt 1–908 Author chain B; PDBConstruct 1–908; UniProt 1–908 Author chain C; PDBConstruct 1–908; UniProt 1–908 Author chain D; PDBConstruct 1–908; UniProt 1–908

Neuropilin and tolloid-like protein 2

Rattus norvegicus

UniProt C6K2K4

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 × 5 其他Polymer 4 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 1–525 Not recorded Glutamate receptor ionotropic, kainate 2 × 4 (P42260) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 16 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NETO2_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–525; UniProt 1–525

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 7f56

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7f56
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7f56
Deposition date deposition_date2021-06-21
Structure title titleDNQX-bound GluK2-1xNeto2 complex, with asymmetric LBD
Keywords keywordsIonotropic glutamate receptors, Single-pass transmembrane proteins, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier61.75
Radius of gyration Rg (electron density) rg_electron61.87
Forward intensity I(0) i02109220000.00
Molecular weight molecular_weight395570.0 kDa
Excluded volume excluded_volume498960 ų
Envelope volume envelope_volume780740 ų
Hydration-shell volume shell_volume109330 ų
Envelope diameter envelope_diameter202.7
Shell Rg shell_rg60.91
Envelope Rg envelope_rg59.69
Shape Rg shape_rg61.89
Total Rg total_rg61.80
Total atoms total_atoms27834
Residues n_residues3468
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 dmax223.6
Rg (real space) rg_real61.88
Rg uncertainty (real space) rg_real_error2.23
I(0) (real space) i0_real2.1090e+09
I(0) uncertainty (real space) i0_real_error4.6970e+07
Rg (reciprocal space) rg_reciprocal61.63
I(0) (reciprocal space) i0_reciprocal2108000000.0000
Solution quality estimate total_estimate0.8497
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary80.5
Skewness Skewness skewness0.368
Kurtosis Kurtosis kurtosis-0.273
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0007
Highest regularization parameter α highest_alpha124500000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.735; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.838

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)