Crystal Structure of the GluA4 Ligand-Binding domain L651V mutant in complex with glutamate. Determined by X-ray diffraction at 1.9 Å resolution. Released 9 Feb 2010.
Explore 3KEI in 3D Show helices and sheets RCSB PDB PDBe
3KEI contains 32 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 | 2-6 | 5 | 1 |
| β-strand | 9 | 1 | 2 |
| β-strand | 13 | 1 | 2 |
| β-strand | 14-15 | 2 | 3 |
| α-helix | 16 | 1 | |
| α-helix | 19-21 | 3 | |
| α-helix | 24-27 | 4 | |
| β-strand | 28-29 | 2 | 3 |
| α-helix | 31-43 | 13 | |
| β-strand | 47-51 | 5 | 1 |
| β-strand | 60 | 1 | 4 |
| β-strand | 67 | 1 | 4 |
| α-helix | 69-75 | 7 | |
| β-strand | 81-82 | 2 | 1 |
| β-strand | 87 | 1 | 5 |
| α-helix | 90-93 | 4 | |
| β-strand | 96-98 | 3 | 1 |
| α-helix | 99 | 1 | |
| α-helix | 101 | 1 | |
| β-strand | 103-105 | 3 | 5 |
| β-strand | 107-112 | 6 | 6 |
| α-helix | 120-124 | 5 | |
| β-strand | 130-132 | 3 | 6 |
| β-strand | 134 | 1 | 7 |
| α-helix | 138-145 | 8 | |
| α-helix | 149-160 | 12 | |
| β-strand | 167 | 1 | 7 |
| α-helix | 170-179 | 10 | |
| β-strand | 184-189 | 6 | 6 |
| α-helix | 190-197 | 8 | |
| β-strand | 204-207 | 4 | 6 |
| β-strand | 214-216 | 3 | 5 |
| β-strand | 219-221 | 3 | 1 |
| α-helix | 227-239 | 13 | |
| α-helix | 242-247 | 6 | |
| α-helix | 248-252 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 8 |
| β-strand | 9 | 1 | 9 |
| β-strand | 13 | 1 | 9 |
| β-strand | 14-15 | 2 | 10 |
| α-helix | 16 | 1 | |
| α-helix | 19-21 | 3 | |
| α-helix | 24-27 | 4 | |
| β-strand | 28-29 | 2 | 10 |
| α-helix | 31-43 | 13 | |
| β-strand | 47-51 | 5 | 8 |
| β-strand | 60 | 1 | 11 |
| β-strand | 67 | 1 | 11 |
| α-helix | 69-75 | 7 | |
| β-strand | 81-82 | 2 | 8 |
| β-strand | 87 | 1 | 12 |
| α-helix | 90-93 | 4 | |
| β-strand | 96-98 | 3 | 8 |
| α-helix | 99 | 1 | |
| α-helix | 101 | 1 | |
| β-strand | 103-105 | 3 | 12 |
| β-strand | 107-112 | 6 | 13 |
| α-helix | 120-124 | 5 | |
| β-strand | 130-132 | 3 | 13 |
| β-strand | 134 | 1 | 14 |
| α-helix | 138-145 | 8 | |
| α-helix | 149-160 | 12 | |
| β-strand | 167 | 1 | 14 |
| α-helix | 170-179 | 10 | |
| β-strand | 184-189 | 6 | 13 |
| α-helix | 190-196 | 7 | |
| β-strand | 204-207 | 4 | 13 |
| β-strand | 214-216 | 3 | 12 |
| β-strand | 219-221 | 3 | 8 |
| α-helix | 227-239 | 13 | |
| α-helix | 242-247 | 6 | |
| α-helix | 248-252 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glutamate receptor 4 | A, B | protein | 257 | Rattus norvegicus | P19493 (AlphaFold model) |
>3KEI_1 Glutamate receptor 4 (chains A, B) TVVVTTIMESPYVMYKKNHEMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDGKYGAR DADTKIWNGMVGELVYGKAEIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKGTPIESA EDLAKQTEIAYGTVDSGSTKEFFRRSKIAVYEKMWTYMRSAEPSVFTRTTAEGVARVRKS KGKFAFLLESTMNEYTEQRKPCDTMKVGGNLDSKGYGVATPKGSSLRTPVNLAVLKLSEA GVLDKLKNKWWYDKGEC
| ID | Name | Formula | Copies |
|---|---|---|---|
| GLU | Glutamic acid | C5 H9 N O4 | 2 |
Enhanced efficacy without further cleft closure: reevaluating twist as a source of agonist efficacy in AMPA receptors. Birdsey-Benson, A., Gill, A., Henderson, L.P. et al. J Neurosci (2010) 30:1463-1470. DOI 10.1523/JNEUROSCI.4558-09.2010 · PubMed
Other PDB entries of the same protein (UniProt P19493 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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