Crystal structure of amino terminal domain of the NMDA receptor subunit GluN1. Determined by X-ray diffraction at 2.0 Å resolution. Released 15 Jun 2011.
Explore 3QEK in 3D Show helices and sheets RCSB PDB PDBe
3QEK contains 44 α-helices and 34 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 | 24 | 1 | |
| β-strand | 25-33 | 9 | 1 |
| α-helix | 36-52 | 17 | |
| β-strand | 58-66 | 9 | 1 |
| α-helix | 67-68 | 2 | |
| α-helix | 71-77 | 7 | |
| α-helix | 78-82 | 5 | |
| α-helix | 83-85 | 3 | |
| β-strand | 87-92 | 6 | 1 |
| α-helix | 105-112 | 8 | |
| β-strand | 118-120 | 3 | 1 |
| α-helix | 126-129 | 4 | |
| β-strand | 137-139 | 3 | 1 |
| α-helix | 144-146 | 3 | |
| α-helix | 147-157 | 11 | |
| β-strand | 162-168 | 7 | 2 |
| α-helix | 171-184 | 14 | |
| α-helix | 207-210 | 4 | |
| β-strand | 211-218 | 8 | 2 |
| α-helix | 226-233 | 8 | |
| β-strand | 239-243 | 5 | 2 |
| α-helix | 246-258 | 13 | |
| β-strand | 267-269 | 3 | 2 |
| α-helix | 273-275 | 3 | |
| α-helix | 277-280 | 4 | |
| α-helix | 283-284 | 2 | |
| β-strand | 288-292 | 5 | 2 |
| α-helix | 298-317 | 20 | |
| α-helix | 324-326 | 3 | |
| α-helix | 339-347 | 9 | |
| β-strand | 351-354 | 4 | 3 |
| β-strand | 357-359 | 3 | 3 |
| β-strand | 361 | 1 | 4 |
| α-helix | 366 | 1 | |
| β-strand | 367 | 1 | 4 |
| α-helix | 368 | 1 | |
| β-strand | 372-378 | 7 | 2 |
| β-strand | 381-388 | 8 | 2 |
| β-strand | 393-395 | 3 | 2 |
| α-helix | 399-402 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 26-33 | 8 | 5 |
| α-helix | 36-52 | 17 | |
| β-strand | 59-66 | 8 | 5 |
| α-helix | 67-68 | 2 | |
| α-helix | 71-77 | 7 | |
| α-helix | 78-82 | 5 | |
| α-helix | 83-85 | 3 | |
| β-strand | 87-92 | 6 | 5 |
| α-helix | 105-112 | 8 | |
| β-strand | 118-120 | 3 | 5 |
| α-helix | 126-129 | 4 | |
| β-strand | 137-139 | 3 | 5 |
| α-helix | 144-147 | 4 | |
| α-helix | 148-157 | 10 | |
| β-strand | 162-168 | 7 | 6 |
| α-helix | 171-194 | 24 | |
| β-strand | 211-218 | 8 | 6 |
| α-helix | 226-233 | 8 | |
| β-strand | 239-243 | 5 | 6 |
| α-helix | 246-258 | 13 | |
| β-strand | 267-270 | 4 | 6 |
| α-helix | 273-275 | 3 | |
| α-helix | 277-282 | 6 | |
| α-helix | 283-284 | 2 | |
| β-strand | 288-292 | 5 | 6 |
| α-helix | 298-316 | 19 | |
| α-helix | 322-326 | 5 | |
| α-helix | 339-347 | 9 | |
| β-strand | 351-354 | 4 | 7 |
| β-strand | 357-359 | 3 | 7 |
| β-strand | 361 | 1 | 8 |
| α-helix | 366 | 1 | |
| β-strand | 367 | 1 | 8 |
| α-helix | 368 | 1 | |
| β-strand | 372-378 | 7 | 6 |
| β-strand | 381-388 | 8 | 6 |
| β-strand | 393-395 | 3 | 6 |
| α-helix | 399-400 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| NMDA glutamate receptor subunit | A, B | protein | 384 | Xenopus laevis | A0A1L8F5J9 (AlphaFold model) |
>3QEK_1 NMDA glutamate receptor subunit (chains A, B) SDPKIVNIGAVLSTKKHEQIFREAVNQANKRHFTRKIQLQATSVTHRPNAIQMALSVCED LISSQVYAILVSHPPAPTDHLTPTPISYTAGFYRIPVIGLTTRMSIYSDKSIHLSFLRTV PPYSHQALVWFEMMRLFNWNHVILIVSDDHEGRAAQKKLETLLEGKESKSKKRNYENLDQ LSYDNKRGPKADKVLQFEPGTKNLTALLLEAKELEARVIILSASEDDATAVYKSAAMLDM TGAGYVWLVGEREISGSALRYAPDGIIGLQLINGKNESAHISDAVAVVAQAIHELFEMEN ITDPPRGCVGNTNIWKTGPLFKRVLMSSKYPDGVTGRIEFNEDGDRKFAQYSIMNLQNRK LVQVGIFNGSYIIQNDRKIIWPGG
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 4 |
Water and common crystallization additives (K) are not listed.
Subunit arrangement and phenylethanolamine binding in GluN1/GluN2B NMDA receptors. Karakas, E., Simorowski, N., Furukawa, H. Nature (2011) 475:249-253. DOI 10.1038/nature10180 · PubMed
Other PDB entries of the same protein (UniProt A0A1L8F5J9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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