5l1f

AMPA subtype ionotropic glutamate receptor GluA2 in complex with noncompetitive inhibitor Perampanel

Method: X-RAY DIFFRACTION Dmax: 195.3 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 6ZP 2-(6'-oxo-1'-phenyl[1',6'-dihydro[2,3'-bipyridine]]-5'-yl)benzonitrile × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;11-14% (w/v) PEG 6,000, 0.1 M ammonium phosphate and 0.1 M TRIS (pH 7.9-8.0) Resolution 4.00 Å R-free 0.272

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 1–535; 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 5l1f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5l1f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5l1f
Deposition date deposition_date2016-07-29
Structure title titleAMPA subtype ionotropic glutamate receptor GluA2 in complex with noncompetitive inhibitor Perampanel
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_guinier56.66
Radius of gyration Rg (electron density) rg_electron56.94
Forward intensity I(0) i01562290000.00
Molecular weight molecular_weight341410.0 kDa
Excluded volume excluded_volume431210 ų
Envelope volume envelope_volume636030 ų
Hydration-shell volume shell_volume95252 ų
Envelope diameter envelope_diameter192.0
Shell Rg shell_rg57.82
Envelope Rg envelope_rg55.53
Shape Rg shape_rg56.97
Total Rg total_rg56.85
Total atoms total_atoms24073
Residues n_residues3100
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 dmax195.3
Rg (real space) rg_real56.70
Rg uncertainty (real space) rg_real_error1.83
I(0) (real space) i0_real1.5620e+09
I(0) uncertainty (real space) i0_real_error3.3090e+07
Rg (reciprocal space) rg_reciprocal56.60
I(0) (reciprocal space) i0_reciprocal1562000000.0000
Solution quality estimate total_estimate0.8635
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary69.8
Skewness Skewness skewness0.320
Kurtosis Kurtosis kurtosis-0.361
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha123600000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.853; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.665

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id5l1fA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id5l1fA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id5l1fB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id5l1fC01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II

8. Citations (1)

9. Files and Curves (10)