7rz4

Structure of the complex of AMPA receptor GluA2 with auxiliary subunit TARP gamma-5 bound to competitive antagonist ZK 200775

Method: ELECTRON MICROSCOPY Dmax: 221.9 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 25–847 Chain B; UniProt 25–847 Chain C; UniProt 25–847 Chain D; UniProt 25–847 Not recorded ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 24 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;0.1mM ZK was added to the purified protein and incubated on ice for 30 min before sample preparation Resolution 3.60 Å

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 1–817; UniProt 25–847 Author chain B; PDBConstruct 1–817; UniProt 25–847 Author chain C; PDBConstruct 1–817; UniProt 25–847 Author chain D; PDBConstruct 1–817; UniProt 25–847

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 7rz4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7rz4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7rz4
Deposition date deposition_date2021-08-27
Structure title titleStructure of the complex of AMPA receptor GluA2 with auxiliary subunit TARP gamma-5 bound to competitive antagonist ZK 200775
Keywords keywordsAMPA receptor, ion channel, neurotransmission, synapse, TARP gamma-5, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier62.44
Radius of gyration Rg (electron density) rg_electron62.92
Forward intensity I(0) i02173130000.00
Molecular weight molecular_weight411930.0 kDa
Excluded volume excluded_volume523810 ų
Envelope volume envelope_volume816500 ų
Hydration-shell volume shell_volume112550 ų
Envelope diameter envelope_diameter207.2
Shell Rg shell_rg60.33
Envelope Rg envelope_rg60.82
Shape Rg shape_rg62.95
Total Rg total_rg62.74
Total atoms total_atoms28998
Residues n_residues3574
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 dmax221.9
Rg (real space) rg_real62.58
Rg uncertainty (real space) rg_real_error2.46
I(0) (real space) i0_real2.1730e+09
I(0) uncertainty (real space) i0_real_error4.6190e+07
Rg (reciprocal space) rg_reciprocal62.28
I(0) (reciprocal space) i0_reciprocal2172000000.0000
Solution quality estimate total_estimate0.8636
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary71.0
Skewness Skewness skewness0.357
Kurtosis Kurtosis kurtosis-0.415
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha161100000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.810; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.794

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id7rz4A01
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_id7rz4B01
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_id7rz4C01
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_id7rz4D01
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)