6dm1

Open state GluA2 in complex with STZ and blocked by NASPM, after micelle signal subtraction

Method: ELECTRON MICROSCOPY Dmax: 220.7 Å Quality: GOOD

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

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

Homo sapiens

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 GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4 GYY N-[3-({4-[(3-aminopropyl)amino]butyl}amino)propyl]-2-(naphthalen-1-yl)acetamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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-2 subunit

Homo sapiens

UniProt Q9Y698

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 2–208 Chain B; UniProt 2–208 Chain C; UniProt 2–208 Chain D; UniProt 2–208 Not recorded GLU GLUTAMIC ACID × 4 CYZ CYCLOTHIAZIDE × 4 GYY N-[3-({4-[(3-aminopropyl)amino]butyl}amino)propyl]-2-(naphthalen-1-yl)acetamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCG2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 820–1026; UniProt 2–208 Author chain B; PDBConstruct 820–1026; UniProt 2–208 Author chain C; PDBConstruct 820–1026; UniProt 2–208 Author chain D; PDBConstruct 820–1026; UniProt 2–208

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 6dm1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6dm1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6dm1
Deposition date deposition_date2018-06-04
Structure title titleOpen state GluA2 in complex with STZ and blocked by NASPM, after micelle signal subtraction
Keywords keywordsIon channel, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier62.99
Radius of gyration Rg (electron density) rg_electron63.12
Forward intensity I(0) i02582200000.00
Molecular weight molecular_weight441590.0 kDa
Excluded volume excluded_volume558380 ų
Envelope volume envelope_volume891290 ų
Hydration-shell volume shell_volume122020 ų
Envelope diameter envelope_diameter207.5
Shell Rg shell_rg60.84
Envelope Rg envelope_rg61.02
Shape Rg shape_rg63.17
Total Rg total_rg62.90
Total atoms total_atoms31131
Residues n_residues3937
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 dmax220.7
Rg (real space) rg_real63.12
Rg uncertainty (real space) rg_real_error2.50
I(0) (real space) i0_real2.5820e+09
I(0) uncertainty (real space) i0_real_error5.6360e+07
Rg (reciprocal space) rg_reciprocal62.84
I(0) (reciprocal space) i0_reciprocal2581000000.0000
Solution quality estimate total_estimate0.8609
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary70.6
Skewness Skewness skewness0.367
Kurtosis Kurtosis kurtosis-0.438
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha220300000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.811; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.756

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)