5fth

Crystal structure of the GluA2 K738M-T744K LBD in complex with glutamate (zinc form)

Method: X-RAY DIFFRACTION Dmax: 103.0 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 404–527 Chain A; UniProt 653–796 Chain B; UniProt 404–527 Chain B; UniProt 653–796 Fragment:LIGAND BINDING DOMAIN, UNP RESIDUES 404-527,653-796 Mutation:YES GLU GLUTAMIC ACID × 2 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;15% PEG 8,000, 200 MM ZN ACETATE, 100MM MES PH 6.0 Resolution 2.90 Å R-free 0.283
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 404–527 Chain C; UniProt 653–796 Fragment:LIGAND BINDING DOMAIN, UNP RESIDUES 404-527,653-796 Mutation:YES GLU GLUTAMIC ACID × 2 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;15% PEG 8,000, 200 MM ZN ACETATE, 100MM MES PH 6.0 Resolution 2.90 Å R-free 0.283

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 481 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 22–145; UniProt 404–527 Author chain A; PDBConstruct 148–291; UniProt 653–796 Author chain B; PDBConstruct 22–145; UniProt 404–527 Author chain B; PDBConstruct 148–291; UniProt 653–796 Author chain C; PDBConstruct 22–145; UniProt 404–527 Author chain C; PDBConstruct 148–291; 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 5fth

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5fth
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5fth
Deposition date deposition_date2016-01-13
Structure title titleCrystal structure of the GluA2 K738M-T744K LBD in complex with glutamate (zinc form)
Keywords keywordsSIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.17
Radius of gyration Rg (electron density) rg_electron30.58
Forward intensity I(0) i0109104000.00
Molecular weight molecular_weight84570.0 kDa
Excluded volume excluded_volume106760 ų
Envelope volume envelope_volume135260 ų
Hydration-shell volume shell_volume37453 ų
Envelope diameter envelope_diameter110.8
Shell Rg shell_rg37.08
Envelope Rg envelope_rg30.45
Shape Rg shape_rg30.53
Total Rg total_rg31.33
Total atoms total_atoms5908
Residues n_residues751
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 dmax103.0
Rg (real space) rg_real31.17
Rg uncertainty (real space) rg_real_error0.85
I(0) (real space) i0_real1.0910e+08
I(0) uncertainty (real space) i0_real_error1.7980e+06
Rg (reciprocal space) rg_reciprocal31.17
I(0) (reciprocal space) i0_reciprocal109100000.0000
Solution quality estimate total_estimate0.8934
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.3
Skewness Skewness skewness0.340
Kurtosis Kurtosis kurtosis-0.370
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27090000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.893; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.962

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_idd5ftha_
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_idd5fthb_
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_idd5fthc_
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_id5fthA01
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_id5fthA02
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_id5fthB01
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_id5fthB02
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_id5fthC01
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_id5fthC02
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)