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.
Explore 3TKD in 3D Show helices and sheets RCSB PDB PDBe
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.
| 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 | 20 | 1 | |
| 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 | 134-136 | 3 | 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 | 194-201 | 8 | |
| β-strand | 208-211 | 4 | 6 |
| β-strand | 218-220 | 3 | 5 |
| β-strand | 223-225 | 3 | 1 |
| α-helix | 231-243 | 13 | |
| α-helix | 246-251 | 6 | |
| α-helix | 252-256 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-10 | 6 | 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 | 50-55 | 6 | 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 | 194-201 | 8 | |
| β-strand | 208-211 | 4 | 13 |
| β-strand | 218-220 | 3 | 12 |
| β-strand | 223-225 | 3 | 8 |
| α-helix | 231-243 | 13 | |
| α-helix | 246-254 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glutamate receptor 2 | A, B | protein | 263 | Rattus norvegicus | P19491 (AlphaFold model) |
>3TKD_1 GLUTAMATE RECEPTOR 2 (chains A, B) GANKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGK YGARDADTKIWNGMVGELVYGKADIAIAPLTITYVREEVIDFSKPFMSLGISIMIKKGTP IESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVAR VRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGNAVNLAVLK LSEQGLLDKLKNKWWYDKGECGS
Water and common crystallization additives (SO4, GOL) are not listed.
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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