1mxv

crystal titration experiments (AMPA co-crystals soaked in 10 mM BrW)

Method: X-RAY DIFFRACTION Dmax: 101.3 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 413–527 Chain A; UniProt 653–796 Chain C; UniProt 413–527 Chain C; UniProt 653–796 Fragment:LIGAND BINDING CORE (S1S2J) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.95 Å R-free 0.248
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 413–527 Chain B; UniProt 653–796 Fragment:LIGAND BINDING CORE (S1S2J) ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.95 Å R-free 0.248
3 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 413–527 Chain A; UniProt 653–796 Chain B; UniProt 413–527 Chain B; UniProt 653–796 Chain C; UniProt 413–527 Chain C; UniProt 653–796 Fragment:LIGAND BINDING CORE (S1S2J) ZN ZINC ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;PEG8000, zinc acetate, sodium cacodylate, pH 6.5 and AMPA, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.95 Å R-free 0.248

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 480 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 3–117; UniProt 413–527 Author chain A; PDBConstruct 120–263; UniProt 653–796 Author chain B; PDBConstruct 3–117; UniProt 413–527 Author chain B; PDBConstruct 120–263; UniProt 653–796 Author chain C; PDBConstruct 3–117; UniProt 413–527 Author chain C; PDBConstruct 120–263; UniProt 653–796

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 1mxv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1mxv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1mxv
Deposition date deposition_date2002-10-03
Structure title titlecrystal titration experiments (AMPA co-crystals soaked in 10 mM BrW)
Keywords keywords;IONOTROPIC GLUTAMATE RECEPTOR, GLUR2, LIGAND BINDING CORE, S1S2, PARTIAL AGONIST, Bromo-WILLARDIINE, AMPA, crystal titration, membrane protein ;; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.27
Radius of gyration Rg (electron density) rg_electron30.60
Forward intensity I(0) i0110198000.00
Molecular weight molecular_weight84121.0 kDa
Excluded volume excluded_volume105770 ų
Envelope volume envelope_volume133760 ų
Hydration-shell volume shell_volume37228 ų
Envelope diameter envelope_diameter108.8
Shell Rg shell_rg36.79
Envelope Rg envelope_rg30.34
Shape Rg shape_rg30.57
Total Rg total_rg31.28
Total atoms total_atoms5886
Residues n_residues775
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 dmax101.3
Rg (real space) rg_real31.29
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real1.1020e+08
I(0) uncertainty (real space) i0_real_error1.8310e+06
Rg (reciprocal space) rg_reciprocal31.28
I(0) (reciprocal space) i0_reciprocal110200000.0000
Solution quality estimate total_estimate0.8935
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.8
Skewness Skewness skewness0.356
Kurtosis Kurtosis kurtosis-0.388
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19370000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.908; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.907

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1mxva_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamilyc.94.1 — Periplasmic binding protein-like II
Family Family familyc.94.1.1 — Phosphate binding protein-like
Domain ID domain_idd1mxvb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamilyc.94.1 — Periplasmic binding protein-like II
Family Family familyc.94.1.1 — Phosphate binding protein-like
Domain ID domain_idd1mxvc_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamilyc.94.1 — Periplasmic binding protein-like II
Family Family familyc.94.1.1 — Phosphate binding protein-like

CATH v4.4 (6 domains)

Domain ID domain_id1mxvA01
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_id1mxvA02
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_id1mxvB01
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_id1mxvB02
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_id1mxvC01
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_id1mxvC02
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 (2)

9. Files and Curves (10)