Crystal structure of the GluA2 LBD (L483Y-N754S-L758V) in complex with glutamate. Determined by X-ray diffraction at 1.44 Å resolution. Released 13 Sept 2017.
Explore 5NS9 in 3D Show helices and sheets RCSB PDB PDBe
5NS9 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| 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 |
| β-strand | 91 | 1 | 5 |
| 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 | 124-128 | 5 | |
| 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 | 230-244 | 15 | |
| α-helix | 246-252 | 7 | |
| α-helix | 253-257 | 5 |
| 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 | 23-25 | 3 | |
| α-helix | 28-31 | 4 | |
| 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 | 134-136 | 3 | 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 | 194-200 | 7 | |
| β-strand | 208-211 | 4 | 13 |
| β-strand | 218-220 | 3 | 12 |
| β-strand | 223-225 | 3 | 8 |
| α-helix | 230-243 | 14 | |
| α-helix | 246-251 | 6 | |
| α-helix | 252-256 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glutamate receptor 2,Glutamate receptor 2 | A, B | protein | 292 | Rattus norvegicus | P19491 (AlphaFold model) |
>5NS9_1 Glutamate receptor 2,Glutamate receptor 2 (chains A, B) MHHHHHHHHSSGLVPRGSAMGSGNDTSRGANKTVVVTTILESPYVMMKKNHEMLEGNERY EGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTI TYVREEVIDFSKPFMSLGISIMIKKGTPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKI AVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVG GNLDSKGYGIATPKGSSLGNAVNLAVLKLSEQGVLDKLKNKWWYDKGECGSG
Water and common crystallization additives (NA, SO4, 1PE) are not listed.
Unitary Properties of AMPA Receptors with Reduced Desensitization. Zhang, W., Eibl, C., Weeks, A.M. et al. Biophys J (2017) 113:2218-2235. DOI 10.1016/j.bpj.2017.07.030 · 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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