3kfm

Crystal Structure of the GluA4 Ligand-Binding domain L651V mutant in complex with kainate

Method: X-RAY DIFFRACTION Dmax: 62.3 Å Quality: GOOD

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

Glutamate receptor 4

Rattus norvegicus

UniProt P19493

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 416–528 Chain A; UniProt 654–795 Fragment:ligand binding domain Mutation:L134V KAI 3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5;291 K;18% PEG 8000, 0.1M Na-Acetate, 0.2M Ammonium Sulphate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.20 Å R-free 0.274

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.

25 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRIA4_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–113; UniProt 416–528 Author chain A; PDBConstruct 116–257; UniProt 654–795

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 3kfm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3kfm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3kfm
Deposition date deposition_date2009-10-27
Structure title titleCrystal Structure of the GluA4 Ligand-Binding domain L651V mutant in complex with kainate
Keywords keywords;GluA4, AMPA receptor, ligand-gated ion channel, ligand-binding domain, L651V, kainate, Alternative splicing, Cell junction, Cell membrane, Glycoprotein, Ion transport, Ionic channel, Lipoprotein, Membrane, Palmitate, Postsynaptic cell membrane, Receptor, Synapse, 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_guinier19.61
Radius of gyration Rg (electron density) rg_electron18.60
Forward intensity I(0) i014046600.00
Molecular weight molecular_weight28901.0 kDa
Excluded volume excluded_volume36554 ų
Envelope volume envelope_volume42189 ų
Hydration-shell volume shell_volume18906 ų
Envelope diameter envelope_diameter63.7
Shell Rg shell_rg24.77
Envelope Rg envelope_rg18.91
Shape Rg shape_rg18.57
Total Rg total_rg19.60
Total atoms total_atoms2028
Residues n_residues257
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 dmax62.3
Rg (real space) rg_real19.52
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real1.4050e+07
I(0) uncertainty (real space) i0_real_error1.8500e+05
Rg (reciprocal space) rg_reciprocal19.53
I(0) (reciprocal space) i0_reciprocal14050000.0000
Solution quality estimate total_estimate0.8217
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.7
Skewness Skewness skewness0.204
Kurtosis Kurtosis kurtosis-0.437
Angular range angular_range— – 0.4050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3102000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.894; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3kfma_
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 (2 domains)

Domain ID domain_id3kfmA01
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_id3kfmA02
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)