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9b35

Ligand-binding and transmembrane domains of kainate receptor GluK2 in the open state, a complex with agonist glutamate and positive allosteric modulator BPAM344

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

Glutamate receptor ionotropic, kainate 2

Rattus norvegicus

UniProt P42260

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 4 GLUTAMIC ACID × 4 Consistent with protein count

Other States of the Same Protein in the Database

Monomer
1s50 2i0b

2 assemblies

Homodimer
1s7y 1tt1 2i0b 2i0c 2xxr 2xxt 2xxu 2xxv 2xxw 2xxx 2xxx 2xxy

35 assemblies; showing the first 12

Homotetramer
1s9t 1sd3 4uqq 5kuf 5kuh 9b35 9c5y 9c5z 9c60 9caz 9dxt 9mzr

12 assemblies

Other homooligomers

None

Heteromeric or nucleic-acid complex
3qlu 3qlu 3qlv 3qlv 3qlv 3qlv 3qlv 3qlv 3qlv 3qlv 5cmm 7f56

58 assemblies; showing the first 12

View Construct and Data Evidence
UniProt name GRIK2_RAT
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–908； UniProt 1–908 Author chain B； PDBConstruct 1–908； UniProt 1–908 Author chain C； PDBConstruct 1–908； UniProt 1–908 Author chain D； PDBConstruct 1–908； UniProt 1–908

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_id9b35
Deposition date deposition_date2024-03-18
Structure title titleLigand-binding and transmembrane domains of kainate receptor GluK2 in the open state, a complex with agonist glutamate and positive allosteric modulator BPAM344
Keywords keywords;kainate receptor, GluK2, positive allosteric modulator, BPAM344, open, glutamate, LBD-TMD, ligand-binding domain, transmembrane domain, MEMBRANE PROTEIN ;; MEMBRANE 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.

9b35__assembly_1__model_1

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

Download this curve (.dat)

9b35__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.

9b35__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）45.35 Å
Rg (electron density)44.92 Å
Total Rg45.19 Å
Atom count14112
Residues1776
Excluded volume253960 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9b35__assembly_1__model_1 tetrameric （4） 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)