Crystal structure of the GluA2 K738M-T744K LBD in complex with glutamate (lithium form). Determined by X-ray diffraction at 1.35 Å resolution. Released 3 Feb 2016.
Explore 5FTI in 3D Show helices and sheets RCSB PDB PDBe
5FTI contains 32 α-helices and 38 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 |
|---|---|---|---|
| α-helix | 393-394 | 2 | |
| β-strand | 395-399 | 5 | 1 |
| β-strand | 407-408 | 2 | 2 |
| α-helix | 412-414 | 3 | |
| α-helix | 417-420 | 4 | |
| β-strand | 421-422 | 2 | 2 |
| α-helix | 424-436 | 13 | |
| β-strand | 440-444 | 5 | 1 |
| β-strand | 453 | 1 | 3 |
| β-strand | 460 | 1 | 3 |
| α-helix | 462-468 | 7 | |
| β-strand | 474-475 | 2 | 1 |
| β-strand | 480 | 1 | 4 |
| α-helix | 483-486 | 4 | |
| β-strand | 489-491 | 3 | 1 |
| α-helix | 492 | 1 | |
| α-helix | 494 | 1 | |
| β-strand | 496-498 | 3 | 4 |
| β-strand | 500-505 | 6 | 5 |
| α-helix | 636-640 | 5 | |
| β-strand | 646-649 | 4 | 5 |
| β-strand | 650 | 1 | 6 |
| α-helix | 654-661 | 8 | |
| α-helix | 665-676 | 12 | |
| β-strand | 683 | 1 | 6 |
| α-helix | 686-695 | 10 | |
| β-strand | 700-705 | 6 | 5 |
| α-helix | 706-713 | 8 | |
| β-strand | 720-723 | 4 | 5 |
| β-strand | 730-732 | 3 | 4 |
| β-strand | 735-737 | 3 | 1 |
| α-helix | 743-756 | 14 | |
| α-helix | 758-763 | 6 | |
| α-helix | 764-768 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 395-399 | 5 | 7 |
| β-strand | 402 | 1 | 8 |
| β-strand | 406 | 1 | 8 |
| β-strand | 407-408 | 2 | 9 |
| α-helix | 409 | 1 | |
| α-helix | 412-414 | 3 | |
| α-helix | 417-420 | 4 | |
| β-strand | 421-422 | 2 | 9 |
| α-helix | 424-436 | 13 | |
| β-strand | 440-444 | 5 | 7 |
| β-strand | 453 | 1 | 10 |
| β-strand | 460 | 1 | 10 |
| α-helix | 462-468 | 7 | |
| β-strand | 474-475 | 2 | 7 |
| β-strand | 480 | 1 | 11 |
| α-helix | 483-486 | 4 | |
| β-strand | 489-491 | 3 | 7 |
| α-helix | 492 | 1 | |
| α-helix | 494 | 1 | |
| β-strand | 496-498 | 3 | 11 |
| β-strand | 500-505 | 6 | 12 |
| α-helix | 636-640 | 5 | |
| β-strand | 646-648 | 3 | 12 |
| β-strand | 650 | 1 | 13 |
| α-helix | 654-661 | 8 | |
| α-helix | 665-676 | 12 | |
| β-strand | 683 | 1 | 13 |
| α-helix | 686-695 | 10 | |
| β-strand | 700-705 | 6 | 12 |
| α-helix | 706-713 | 8 | |
| β-strand | 720-723 | 4 | 12 |
| β-strand | 730-732 | 3 | 11 |
| β-strand | 735-737 | 3 | 7 |
| α-helix | 743-755 | 13 | |
| α-helix | 758-763 | 6 | |
| α-helix | 764-768 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glutamate receptor 2 | A, B | protein | 291 | RATTUS NORVEGICUS | P19491 (AlphaFold model) |
>5FTI_1 GLUTAMATE RECEPTOR 2 (chains A, B) MHHHHHHHHSSGLVPRGSAMGSGNDTSRGANKTVVVTTILESPYVMMKKNHEMLEGNERY EGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTI TLVREEVIDFSKPFMSLGISIMIKKGTPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKI AVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVG GNLDSKGYGIATPMGSSLGKPVNLAVLKLSEQGVLDKLKNKWWYDKGECGA
Water and common crystallization additives (SO4, GOL) are not listed.
Distinct Structural Pathways Coordinate the Activation of Ampa Receptor-Auxiliary Subunit Complexes. Dawe, G.B., Musgaard, M., Aurousseau, M.R.P. et al. Neuron (2016) 89:1264. DOI 10.1016/J.NEURON.2016.01.038 · 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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