3h5w

Crystal structure of the GluR2-ATD in space group P212121 without solvent

Method: X-RAY DIFFRACTION Dmax: 88.4 Å Quality: EXCELLENT

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 0–383 Chain B; UniProt 0–383 Fragment:UNP residues 21-404 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;277 K;20% PEG3000, 100mM tri-sodium citrate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.69 Å R-free 0.291

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 5–388; UniProt 0–383 Author chain B; PDBConstruct 5–388; UniProt 0–383

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 3h5w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3h5w
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3h5w
Deposition date deposition_date2009-04-22
Structure title titleCrystal structure of the GluR2-ATD in space group P212121 without solvent
Keywords keywords;Glutamate receptor, Ligand-gated ion channel, synapse, Alternative splicing, Cell junction, Cell membrane, Endoplasmic reticulum, Glycoprotein, Ion transport, Ionic channel, Lipoprotein, Membrane, Palmitate, Phosphoprotein, Postsynaptic cell membrane, Receptor, RNA editing, Transmembrane, Transport, TRANSPORT PROTEIN ;; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.78
Radius of gyration Rg (electron density) rg_electron27.66
Forward intensity I(0) i097583800.00
Molecular weight molecular_weight76377.0 kDa
Excluded volume excluded_volume94871 ų
Envelope volume envelope_volume121490 ų
Hydration-shell volume shell_volume35697 ų
Envelope diameter envelope_diameter89.9
Shell Rg shell_rg35.74
Envelope Rg envelope_rg27.57
Shape Rg shape_rg27.67
Total Rg total_rg28.46
Total atoms total_atoms5404
Residues n_residues737
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 dmax88.4
Rg (real space) rg_real28.67
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real9.7580e+07
I(0) uncertainty (real space) i0_real_error1.3550e+06
Rg (reciprocal space) rg_reciprocal28.72
I(0) (reciprocal space) i0_reciprocal97590000.0000
Solution quality estimate total_estimate0.9103
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.4
Skewness Skewness skewness0.158
Kurtosis Kurtosis kurtosis-0.590
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha47740000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.958; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.956

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3h5wa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.93 — Periplasmic binding protein-like I
Superfamily Superfamily superfamilyc.93.1 — Periplasmic binding protein-like I
Family Family familyc.93.1.1 — L-arabinose binding protein-like
Domain ID domain_idd3h5wb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.93 — Periplasmic binding protein-like I
Superfamily Superfamily superfamilyc.93.1 — Periplasmic binding protein-like I
Family Family familyc.93.1.1 — L-arabinose binding protein-like

CATH v4.4 (4 domains)

Domain ID domain_id3h5wA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id3h5wA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id3h5wB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id3h5wB02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator

8. Citations (1)

9. Files and Curves (10)