5vhw

GluA2-0xGSG1L bound to ZK

Method: ELECTRON MICROSCOPY Dmax: 202.0 Å Quality: GOOD

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

Glutamate receptor 2,Germ cell-specific gene 1-like protein

Rattus norvegicus

UniProt D3ZK93

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 2–238 Chain B; UniProt 2–238 Chain C; UniProt 2–238 Chain D; UniProt 2–238 Not recorded ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.80 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 GSG1L_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 821–1057; UniProt 2–238 Author chain B; PDBConstruct 821–1057; UniProt 2–238 Author chain C; PDBConstruct 821–1057; UniProt 2–238 Author chain D; PDBConstruct 821–1057; UniProt 2–238

Glutamate receptor 2,Germ cell-specific gene 1-like protein

Rattus norvegicus

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 ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.80 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

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 5vhw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5vhw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5vhw
Deposition date deposition_date2017-04-13
Structure title titleGluA2-0xGSG1L bound to ZK
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_guinier57.47
Radius of gyration Rg (electron density) rg_electron57.77
Forward intensity I(0) i01668380000.00
Molecular weight molecular_weight351590.0 kDa
Excluded volume excluded_volume443770 ų
Envelope volume envelope_volume662670 ų
Hydration-shell volume shell_volume98422 ų
Envelope diameter envelope_diameter197.0
Shell Rg shell_rg58.05
Envelope Rg envelope_rg56.08
Shape Rg shape_rg57.80
Total Rg total_rg57.67
Total atoms total_atoms24756
Residues n_residues3126
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 dmax202.0
Rg (real space) rg_real57.54
Rg uncertainty (real space) rg_real_error2.13
I(0) (real space) i0_real1.6680e+09
I(0) uncertainty (real space) i0_real_error3.3480e+07
Rg (reciprocal space) rg_reciprocal57.40
I(0) (reciprocal space) i0_reciprocal1668000000.0000
Solution quality estimate total_estimate0.8612
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary74.8
Skewness Skewness skewness0.340
Kurtosis Kurtosis kurtosis-0.338
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha113700000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.815; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.766

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)