Crystal structure of the GLUR2 ligand binding core (S1S2J, flip variant) in the apo state. Determined by X-ray diffraction at 1.41 Å resolution. Released 20 Aug 2014.
Explore 4U2R in 3D Show helices and sheets RCSB PDB PDBe
4U2R contains 62 α-helices and 78 β-strands across 4 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 |
|---|---|---|---|
| β-strand | 6-10 | 5 | 7 |
| β-strand | 13 | 1 | 8 |
| β-strand | 17 | 1 | 8 |
| β-strand | 18-19 | 2 | 9 |
| α-helix | 23-25 | 3 | |
| α-helix | 28-31 | 4 | |
| β-strand | 32-33 | 2 | 9 |
| α-helix | 35-47 | 13 | |
| β-strand | 51-55 | 5 | 7 |
| β-strand | 64 | 1 | 10 |
| β-strand | 71 | 1 | 10 |
| α-helix | 73-79 | 7 | |
| β-strand | 85-86 | 2 | 7 |
| β-strand | 91 | 1 | 11 |
| α-helix | 94-97 | 4 | |
| β-strand | 101-102 | 2 | 7 |
| α-helix | 103 | 1 | |
| α-helix | 105 | 1 | |
| β-strand | 107-109 | 3 | 11 |
| β-strand | 111-116 | 6 | 12 |
| α-helix | 124-128 | 5 | |
| β-strand | 134-136 | 3 | 12 |
| β-strand | 138 | 1 | 13 |
| α-helix | 142-149 | 8 | |
| α-helix | 153-164 | 12 | |
| β-strand | 171 | 1 | 13 |
| α-helix | 174-183 | 10 | |
| β-strand | 188-193 | 6 | 12 |
| α-helix | 194-201 | 8 | |
| β-strand | 208-211 | 4 | 12 |
| β-strand | 218-220 | 3 | 11 |
| β-strand | 223-224 | 2 | 7 |
| α-helix | 231-243 | 13 | |
| α-helix | 246-252 | 7 | |
| α-helix | 253-257 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-10 | 5 | 1 |
| β-strand | 18-19 | 2 | 2 |
| α-helix | 23-25 | 3 | |
| α-helix | 28-31 | 4 | |
| β-strand | 32-33 | 2 | 2 |
| α-helix | 35-47 | 13 | |
| β-strand | 51-55 | 5 | 1 |
| β-strand | 64 | 1 | 3 |
| β-strand | 71 | 1 | 3 |
| α-helix | 73-79 | 7 | |
| β-strand | 85-86 | 2 | 1 |
| β-strand | 91 | 1 | 4 |
| α-helix | 94-97 | 4 | |
| β-strand | 100-102 | 3 | 1 |
| α-helix | 103 | 1 | |
| α-helix | 105 | 1 | |
| β-strand | 107-109 | 3 | 4 |
| β-strand | 111-116 | 6 | 5 |
| α-helix | 124-128 | 5 | |
| β-strand | 134-136 | 3 | 5 |
| β-strand | 138 | 1 | 6 |
| α-helix | 142-149 | 8 | |
| α-helix | 153-164 | 12 | |
| β-strand | 171 | 1 | 6 |
| α-helix | 174-183 | 10 | |
| β-strand | 188-193 | 6 | 5 |
| α-helix | 194-201 | 8 | |
| β-strand | 208-211 | 4 | 5 |
| β-strand | 218-220 | 3 | 4 |
| β-strand | 223-225 | 3 | 1 |
| α-helix | 231-243 | 13 | |
| α-helix | 246-252 | 7 | |
| α-helix | 253-257 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-5 | 2 | |
| β-strand | 6-10 | 5 | 14 |
| β-strand | 13 | 1 | 15 |
| β-strand | 17 | 1 | 15 |
| β-strand | 18-19 | 2 | 16 |
| α-helix | 23-25 | 3 | |
| α-helix | 28-31 | 4 | |
| β-strand | 32-33 | 2 | 16 |
| α-helix | 35-47 | 13 | |
| β-strand | 51-55 | 5 | 14 |
| β-strand | 64 | 1 | 17 |
| β-strand | 71 | 1 | 17 |
| α-helix | 73-79 | 7 | |
| β-strand | 85-86 | 2 | 14 |
| β-strand | 91 | 1 | 18 |
| α-helix | 94-97 | 4 | |
| β-strand | 101-102 | 2 | 14 |
| α-helix | 103 | 1 | |
| α-helix | 105 | 1 | |
| β-strand | 107-109 | 3 | 18 |
| β-strand | 111-116 | 6 | 19 |
| α-helix | 124-128 | 5 | |
| β-strand | 134-136 | 3 | 19 |
| β-strand | 138 | 1 | 20 |
| α-helix | 142-149 | 8 | |
| α-helix | 153-164 | 12 | |
| β-strand | 171 | 1 | 20 |
| α-helix | 174-183 | 10 | |
| β-strand | 188-193 | 6 | 19 |
| α-helix | 194-201 | 8 | |
| β-strand | 208-211 | 4 | 19 |
| β-strand | 218-220 | 3 | 18 |
| β-strand | 223-224 | 2 | 14 |
| α-helix | 231-243 | 13 | |
| α-helix | 246-252 | 7 | |
| α-helix | 253-257 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-5 | 2 | |
| β-strand | 6-10 | 5 | 21 |
| β-strand | 13 | 1 | 22 |
| β-strand | 17 | 1 | 22 |
| β-strand | 18-19 | 2 | 23 |
| α-helix | 23-25 | 3 | |
| α-helix | 28-31 | 4 | |
| β-strand | 32-33 | 2 | 23 |
| α-helix | 35-47 | 13 | |
| β-strand | 51-55 | 5 | 21 |
| β-strand | 64 | 1 | 24 |
| β-strand | 71 | 1 | 24 |
| α-helix | 73-79 | 7 | |
| β-strand | 85-86 | 2 | 21 |
| β-strand | 91 | 1 | 25 |
| α-helix | 94-97 | 4 | |
| β-strand | 100-102 | 3 | 21 |
| α-helix | 103 | 1 | |
| α-helix | 105 | 1 | |
| β-strand | 107-109 | 3 | 25 |
| β-strand | 111-116 | 6 | 26 |
| α-helix | 124-128 | 5 | |
| β-strand | 134-136 | 3 | 26 |
| β-strand | 138 | 1 | 27 |
| α-helix | 142-149 | 8 | |
| α-helix | 153-164 | 12 | |
| β-strand | 171 | 1 | 27 |
| α-helix | 174-183 | 10 | |
| β-strand | 188-193 | 6 | 26 |
| α-helix | 194-201 | 8 | |
| β-strand | 208-211 | 4 | 26 |
| β-strand | 218-220 | 3 | 25 |
| β-strand | 223-225 | 3 | 21 |
| α-helix | 231-243 | 13 | |
| α-helix | 246-252 | 7 | |
| α-helix | 253-257 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glutamate receptor 2 | A, B, C, D | protein | 263 | Rattus norvegicus | P19491 (AlphaFold model) |
>4U2R_1 Glutamate receptor 2 (chains A, B, C, D) GANKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGK YGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKGTP IESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVAR VRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGTPVNLAVLK LSEQGVLDKLKNKWWYDKGECGS
Structure and Dynamics of AMPA Receptor GluA2 in Resting, Pre-Open, and Desensitized States. Durr, K.L., Chen, L., Stein, R.A. et al. Cell (2014) 158:778-792. DOI 10.1016/j.cell.2014.07.023 · 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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