5n6p

AMPA receptor NTD mutant

Method: X-RAY DIFFRACTION Dmax: 73.7 Å Quality: REASONABLE

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 25–400 Mutation:K73C D134C NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;291 K;16-20% PEG3350, 200 mM sodium formate Resolution 2.80 Å R-free 0.249

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 32–407; UniProt 25–400

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 5n6p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5n6p
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5n6p
Deposition date deposition_date2017-02-15
Structure title titleAMPA receptor NTD mutant
Keywords keywordsampa, ntd, glutamate receptor, 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_guinier22.73
Radius of gyration Rg (electron density) rg_electron21.58
Forward intensity I(0) i029131900.00
Molecular weight molecular_weight41561.0 kDa
Excluded volume excluded_volume52060 ų
Envelope volume envelope_volume62164 ų
Hydration-shell volume shell_volume24001 ų
Envelope diameter envelope_diameter75.0
Shell Rg shell_rg28.51
Envelope Rg envelope_rg21.83
Shape Rg shape_rg21.58
Total Rg total_rg22.48
Total atoms total_atoms2933
Residues n_residues369
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 dmax73.7
Rg (real space) rg_real22.68
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real2.9130e+07
I(0) uncertainty (real space) i0_real_error3.4490e+05
Rg (reciprocal space) rg_reciprocal22.69
I(0) (reciprocal space) i0_reciprocal29130000.0000
Solution quality estimate total_estimate0.7177
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.8
Skewness Skewness skewness0.315
Kurtosis Kurtosis kurtosis-0.313
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha7804000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.867; Stabil: 1.000; Sysdev: 0.242; Positv: 1.000; Valcen: 1.000; Smooth: 0.996

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_idd5n6pa_
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 (2 domains)

Domain ID domain_id5n6pA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id5n6pA02
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)