5kk2

Architecture of fully occupied GluA2 AMPA receptor - TARP complex elucidated by single particle cryo-electron microscopy

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Glutamate receptor 2

Rattus norvegicus

UniProt P19491

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 8 Voltage-dependent calcium channel gamma-2 subunit × 4 (Q71RJ2) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name GRIA2_RAT
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–889; UniProt 1–883 Author chain B; PDBConstruct 1–889; UniProt 1–883 Author chain C; PDBConstruct 1–889; UniProt 1–883 Author chain D; PDBConstruct 1–889; UniProt 1–883

Voltage-dependent calcium channel gamma-2 subunit

Rattus norvegicus

UniProt Q71RJ2

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 8 Glutamate receptor 2 × 4 (P19491) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name CCG2_RAT
Isoform —
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–323; UniProt 1–323 Author chain F; PDBConstruct 1–323; UniProt 1–323 Author chain G; PDBConstruct 1–323; UniProt 1–323 Author chain H; PDBConstruct 1–323; UniProt 1–323

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id5kk2
Deposition date deposition_date2016-06-20
Structure title titleArchitecture of fully occupied GluA2 AMPA receptor - TARP complex elucidated by single particle cryo-electron microscopy
Keywords keywords;Tetrameric, ionotropic, glutamate receptors, GluA2 - TARP gamma2 complex, fully occupied, antagonist-bound state, MEMBRANE PROTEIN, TRANSPORT PROTEIN, SIGNALING PROTEIN ;; MEMBRANE PROTEIN, TRANSPORT PROTEIN, SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

5kk2__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

5kk2__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

5kk2__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)46.29 Å
Rg (electron density)45.42 Å
Total Rg45.51 Å
Atom count14639
Residues2309
Excluded volume255470 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 5kk2__assembly_1__model_1 octameric (8) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (2)

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7. Citations (1)