3TKD: GluA2 ligand-binding domain

Crystal structure of the GluA2 ligand-binding domain (S1S2J-L483Y-N754S) in complex with glutamate and cyclothiazide at 1.45 A resolution. Determined by X-ray diffraction at 1.45 Å resolution. Released 21 Sept 2011.

Method
X-ray diffraction
Resolution
1.45 Å
Organism
Rattus norvegicus
Chains
2
Atoms
4,982
Mol. weight
60.42 kDa
Ligands
GLU, CYZ
Released
21 Sept 2011

Explore 3TKD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3TKD contains 33 α-helices and 40 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 16 helices, 20 β-strands

ElementResiduesLengthSheet
β-strand6-1051
β-strand1312
β-strand1712
β-strand18-1923
α-helix201
α-helix23-253
α-helix28-314
β-strand32-3323
α-helix35-4713
β-strand51-5551
β-strand6414
β-strand7114
α-helix73-797
β-strand85-8621
β-strand9115
α-helix94-974
β-strand100-10231
α-helix1031
α-helix1051
β-strand107-10935
β-strand111-11666
α-helix124-1285
β-strand134-13636
β-strand13817
α-helix142-1498
α-helix153-16412
β-strand17117
α-helix174-18310
β-strand188-19366
α-helix194-2018
β-strand208-21146
β-strand218-22035
β-strand223-22531
α-helix231-24313
α-helix246-2516
α-helix252-2565
Chain B: 17 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand5-1068
β-strand1319
β-strand1719
β-strand18-19210
α-helix201
α-helix23-253
α-helix28-314
β-strand32-33210
α-helix35-4713
β-strand50-5568
β-strand64111
β-strand71111
α-helix73-797
β-strand85-8628
α-helix901
β-strand91112
α-helix921
α-helix94-974
β-strand100-10238
α-helix1031
α-helix1051
β-strand107-109312
β-strand111-116613
α-helix124-1285
β-strand134-136313
β-strand138114
α-helix142-1498
α-helix153-16412
β-strand171114
α-helix174-18310
β-strand188-193613
α-helix194-2018
β-strand208-211413
β-strand218-220312
β-strand223-22538
α-helix231-24313
α-helix246-2549

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Glutamate receptor 2A, Bprotein263Rattus norvegicusP19491 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3TKD_1 GLUTAMATE RECEPTOR 2 (chains A, B)
GANKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGK
YGARDADTKIWNGMVGELVYGKADIAIAPLTITYVREEVIDFSKPFMSLGISIMIKKGTP
IESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVAR
VRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGNAVNLAVLK
LSEQGLLDKLKNKWWYDKGECGS

Ligands and cofactors

IDNameFormulaCopies
GLUGlutamic acidC5 H9 N O42
CYZCyclothiazideC14 H16 Cl N3 O4 S22

Water and common crystallization additives (SO4, GOL) are not listed.

Primary citation

Thermodynamics and structural analysis of positive allosteric modulation of the ionotropic glutamate receptor GluA2. Krintel, C., Frydenvang, K., Olsen, L. et al. Biochem J (2012) 441:173-178. DOI 10.1042/BJ20111221 · PubMed

Other PDB entries of the same protein (UniProt P19491 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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