1M5E: GLUR2 ligand binding core

X-ray structure of the GLUR2 ligand binding core (S1S2J) in complex with acpa at 1.46 a resolution. Determined by X-ray diffraction at 1.46 Å resolution. Released 18 Sept 2002.

Method
X-ray diffraction
Resolution
1.46 Å
Organism
Rattus norvegicus
Chains
3
Atoms
7,182
Mol. weight
88.89 kDa
Ligands
AM1, ZN
Released
18 Sept 2002

Explore 1M5E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1M5E contains 52 α-helices and 60 β-strands across 3 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: 18 helices, 20 β-strands

ElementResiduesLengthSheet
α-helix51
β-strand6-1051
β-strand1312
β-strand1712
β-strand18-1923
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
α-helix901
β-strand9115
α-helix921
α-helix94-974
β-strand100-10231
α-helix1031
α-helix1051
β-strand107-10935
β-strand111-11666
α-helix124-1296
β-strand134-13746
β-strand13817
α-helix142-1498
α-helix153-16412
β-strand17117
α-helix174-18310
β-strand188-19366
α-helix194-2007
β-strand208-21146
β-strand218-22035
β-strand223-22531
α-helix230-24314
α-helix246-2516
α-helix252-2576
Chain B: 17 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand6-1058
β-strand1319
β-strand1719
β-strand18-19210
α-helix201
α-helix29-313
β-strand32-33210
α-helix35-4713
β-strand51-5558
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-strand134-137413
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-helix231-24414
α-helix246-2516
α-helix252-2565
Chain C: 17 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand6-10515
β-strand13116
β-strand17116
β-strand18-19217
α-helix23-253
α-helix28-314
β-strand32-33217
α-helix35-4713
β-strand51-55515
β-strand64118
β-strand71118
α-helix73-797
β-strand85-86215
α-helix901
β-strand91119
α-helix921
α-helix94-974
β-strand100-102315
α-helix1031
α-helix1051
β-strand107-109319
β-strand111-116620
α-helix124-1285
β-strand134-137420
β-strand138121
α-helix142-1498
α-helix153-16412
β-strand171121
α-helix174-18310
β-strand188-193620
α-helix194-2007
β-strand208-211420
β-strand218-220319
β-strand223-225315
α-helix230-24314
α-helix246-2516
α-helix252-2565

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Glutamate receptor 2A, B, Cprotein263Rattus norvegicusP19491 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>1M5E_1 Glutamate receptor 2 (chains A, B, C)
GANKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGK
YGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKGTP
IESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVAR
VRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGNAVNLAVLK
LNEQGLLDKLKNKWWYDKGECGS

Ligands and cofactors

IDNameFormulaCopies
AM1(s)-2-amino-3-(3-carboxy-5-methylisoxazol-4-yl)propionic acidC8 H10 N2 O53
ZNZinc ionZn8

Water and common crystallization additives (ACT) are not listed.

Primary citation

Structural Basis for AMPA Receptor Activation and Ligand Selectivity: Crystal Structures of Five Agonist Complexes with the GluR2 Ligand-binding Core. Hogner, A., Kastrup, J.S., Jin, R. et al. J Mol Biol (2002) 322:93-109. DOI 10.1016/S0022-2836(02)00650-2 · 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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