5l1g

AMPA subtype ionotropic glutamate receptor GluA2 in complex with GYKI-Br

Method: X-RAY DIFFRACTION Dmax: 178.2 Å Quality: GOOD

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

Glutamate receptor 2

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 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 25–565 Chain A; UniProt 588–847 Chain B; UniProt 25–565 Chain B; UniProt 588–847 Chain C; UniProt 25–565 Chain C; UniProt 588–847 Chain D; UniProt 25–565 Chain D; UniProt 588–847 Fragment:UNP residues 25-847, with deletions of 397-398, 402-405, 566-587 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 GYB (8R)-5-(4-amino-3-bromophenyl)-N,8-dimethyl-8,9-dihydro-2H,7H-[1,3]dioxolo[4,5-h][2,3]benzodiazepine-7-carboxamide × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;sodium acetate Resolution 4.51 Å R-free 0.295

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
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–535; UniProt 25–565 Author chain A; PDBConstruct 539–798; UniProt 588–847 Author chain B; PDBConstruct 1–535; UniProt 25–565 Author chain B; PDBConstruct 539–798; UniProt 588–847 Author chain C; PDBConstruct 1–535; UniProt 25–565 Author chain C; PDBConstruct 539–798; UniProt 588–847 Author chain D; PDBConstruct 1–535; UniProt 25–565 Author chain D; PDBConstruct 539–798; UniProt 588–847

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 5l1g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5l1g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5l1g
Deposition date deposition_date2016-07-29
Structure title titleAMPA subtype ionotropic glutamate receptor GluA2 in complex with GYKI-Br
Keywords keywordsTransporter, MEMBRANE PROTEIN, TRANSPORT PROTEIN, TRANSPORT PROTEIN-INHIBITOR complex; TRANSPORT PROTEIN/INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier57.12
Radius of gyration Rg (electron density) rg_electron57.36
Forward intensity I(0) i01579120000.00
Molecular weight molecular_weight341940.0 kDa
Excluded volume excluded_volume431310 ų
Envelope volume envelope_volume651580 ų
Hydration-shell volume shell_volume96728 ų
Envelope diameter envelope_diameter193.1
Shell Rg shell_rg58.23
Envelope Rg envelope_rg55.94
Shape Rg shape_rg57.38
Total Rg total_rg57.31
Total atoms total_atoms24087
Residues n_residues3101
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 dmax178.2
Rg (real space) rg_real57.15
Rg uncertainty (real space) rg_real_error2.25
I(0) (real space) i0_real1.5790e+09
I(0) uncertainty (real space) i0_real_error3.4920e+07
Rg (reciprocal space) rg_reciprocal57.07
I(0) (reciprocal space) i0_reciprocal1579000000.0000
Solution quality estimate total_estimate0.8413
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary70.0
Skewness Skewness skewness0.309
Kurtosis Kurtosis kurtosis-0.390
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha117300000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.947; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.093

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)