4u2p

Full-length AMPA subtype ionotropic glutamate receptor GluA2 in the apo state

Method: X-RAY DIFFRACTION Dmax: 194.8 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 25–847 Chain B; UniProt 25–847 Chain C; UniProt 25–847 Chain D; UniProt 25–847 Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277.15 K;0.1 M MES, 5.8-6.2% PEG6000, 5% TMAO, 0.1-0.3 M sodium acetate Resolution 3.24 Å R-free 0.288

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 1–819; UniProt 25–847 Author chain B; PDBConstruct 1–819; UniProt 25–847 Author chain C; PDBConstruct 1–819; UniProt 25–847 Author chain D; PDBConstruct 1–819; 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 4u2p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4u2p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4u2p
Deposition date deposition_date2014-07-17
Structure title titleFull-length AMPA subtype ionotropic glutamate receptor GluA2 in the apo state
Keywords keywordsAMPA receptor, Transport protein, Membrane protein; Transport protein, Membrane protein
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier55.41
Radius of gyration Rg (electron density) rg_electron55.88
Forward intensity I(0) i01408960000.00
Molecular weight molecular_weight317120.0 kDa
Excluded volume excluded_volume397530 ų
Envelope volume envelope_volume614880 ų
Hydration-shell volume shell_volume93846 ų
Envelope diameter envelope_diameter194.8
Shell Rg shell_rg56.82
Envelope Rg envelope_rg54.60
Shape Rg shape_rg55.91
Total Rg total_rg55.81
Total atoms total_atoms22388
Residues n_residues3022
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 dmax194.8
Rg (real space) rg_real55.43
Rg uncertainty (real space) rg_real_error2.05
I(0) (real space) i0_real1.4090e+09
I(0) uncertainty (real space) i0_real_error2.8510e+07
Rg (reciprocal space) rg_reciprocal55.37
I(0) (reciprocal space) i0_reciprocal1409000000.0000
Solution quality estimate total_estimate0.8697
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary69.5
Skewness Skewness skewness0.324
Kurtosis Kurtosis kurtosis-0.345
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha118600000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.829; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.819

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 5 domains

CATH v4.4 (5 domains)

Domain ID domain_id4u2pA01
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_id4u2pB01
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_id4u2pC01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id4u2pC02
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_id4u2pD01
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)