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.
Explore 1M5E in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5 | 1 | |
| β-strand | 6-10 | 5 | 1 |
| β-strand | 13 | 1 | 2 |
| β-strand | 17 | 1 | 2 |
| β-strand | 18-19 | 2 | 3 |
| α-helix | 23-25 | 3 | |
| α-helix | 28-31 | 4 | |
| β-strand | 32-33 | 2 | 3 |
| α-helix | 35-47 | 13 | |
| β-strand | 51-55 | 5 | 1 |
| β-strand | 64 | 1 | 4 |
| β-strand | 71 | 1 | 4 |
| α-helix | 73-79 | 7 | |
| β-strand | 85-86 | 2 | 1 |
| α-helix | 90 | 1 | |
| β-strand | 91 | 1 | 5 |
| α-helix | 92 | 1 | |
| α-helix | 94-97 | 4 | |
| β-strand | 100-102 | 3 | 1 |
| α-helix | 103 | 1 | |
| α-helix | 105 | 1 | |
| β-strand | 107-109 | 3 | 5 |
| β-strand | 111-116 | 6 | 6 |
| α-helix | 124-129 | 6 | |
| β-strand | 134-137 | 4 | 6 |
| β-strand | 138 | 1 | 7 |
| α-helix | 142-149 | 8 | |
| α-helix | 153-164 | 12 | |
| β-strand | 171 | 1 | 7 |
| α-helix | 174-183 | 10 | |
| β-strand | 188-193 | 6 | 6 |
| α-helix | 194-200 | 7 | |
| β-strand | 208-211 | 4 | 6 |
| β-strand | 218-220 | 3 | 5 |
| β-strand | 223-225 | 3 | 1 |
| α-helix | 230-243 | 14 | |
| α-helix | 246-251 | 6 | |
| α-helix | 252-257 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-10 | 5 | 8 |
| β-strand | 13 | 1 | 9 |
| β-strand | 17 | 1 | 9 |
| β-strand | 18-19 | 2 | 10 |
| α-helix | 20 | 1 | |
| α-helix | 29-31 | 3 | |
| β-strand | 32-33 | 2 | 10 |
| α-helix | 35-47 | 13 | |
| β-strand | 51-55 | 5 | 8 |
| β-strand | 64 | 1 | 11 |
| β-strand | 71 | 1 | 11 |
| α-helix | 73-79 | 7 | |
| β-strand | 85-86 | 2 | 8 |
| α-helix | 90 | 1 | |
| β-strand | 91 | 1 | 12 |
| α-helix | 92 | 1 | |
| α-helix | 94-97 | 4 | |
| β-strand | 100-102 | 3 | 8 |
| α-helix | 103 | 1 | |
| α-helix | 105 | 1 | |
| β-strand | 107-109 | 3 | 12 |
| β-strand | 111-116 | 6 | 13 |
| α-helix | 124-128 | 5 | |
| β-strand | 134-137 | 4 | 13 |
| β-strand | 138 | 1 | 14 |
| α-helix | 142-149 | 8 | |
| α-helix | 153-164 | 12 | |
| β-strand | 171 | 1 | 14 |
| α-helix | 174-183 | 10 | |
| β-strand | 188-193 | 6 | 13 |
| α-helix | 194-201 | 8 | |
| β-strand | 208-211 | 4 | 13 |
| β-strand | 218-220 | 3 | 12 |
| β-strand | 223-225 | 3 | 8 |
| α-helix | 231-244 | 14 | |
| α-helix | 246-251 | 6 | |
| α-helix | 252-256 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-10 | 5 | 15 |
| β-strand | 13 | 1 | 16 |
| β-strand | 17 | 1 | 16 |
| β-strand | 18-19 | 2 | 17 |
| α-helix | 23-25 | 3 | |
| α-helix | 28-31 | 4 | |
| β-strand | 32-33 | 2 | 17 |
| α-helix | 35-47 | 13 | |
| β-strand | 51-55 | 5 | 15 |
| β-strand | 64 | 1 | 18 |
| β-strand | 71 | 1 | 18 |
| α-helix | 73-79 | 7 | |
| β-strand | 85-86 | 2 | 15 |
| α-helix | 90 | 1 | |
| β-strand | 91 | 1 | 19 |
| α-helix | 92 | 1 | |
| α-helix | 94-97 | 4 | |
| β-strand | 100-102 | 3 | 15 |
| α-helix | 103 | 1 | |
| α-helix | 105 | 1 | |
| β-strand | 107-109 | 3 | 19 |
| β-strand | 111-116 | 6 | 20 |
| α-helix | 124-128 | 5 | |
| β-strand | 134-137 | 4 | 20 |
| β-strand | 138 | 1 | 21 |
| α-helix | 142-149 | 8 | |
| α-helix | 153-164 | 12 | |
| β-strand | 171 | 1 | 21 |
| α-helix | 174-183 | 10 | |
| β-strand | 188-193 | 6 | 20 |
| α-helix | 194-200 | 7 | |
| β-strand | 208-211 | 4 | 20 |
| β-strand | 218-220 | 3 | 19 |
| β-strand | 223-225 | 3 | 15 |
| α-helix | 230-243 | 14 | |
| α-helix | 246-251 | 6 | |
| α-helix | 252-256 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glutamate receptor 2 | A, B, C | protein | 263 | Rattus norvegicus | P19491 (AlphaFold model) |
>1M5E_1 Glutamate receptor 2 (chains A, B, C) GANKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGK YGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKGTP IESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVAR VRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGNAVNLAVLK LNEQGLLDKLKNKWWYDKGECGS
| ID | Name | Formula | Copies |
|---|---|---|---|
| AM1 | (s)-2-amino-3-(3-carboxy-5-methylisoxazol-4-yl)propionic acid | C8 H10 N2 O5 | 3 |
| ZN | Zinc ion | Zn | 8 |
Water and common crystallization additives (ACT) are not listed.
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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