Crystal structure of amino terminal domains of the nmda receptor subunit GLUN1 and GLUN2B in complex with mk-22. Determined by X-ray diffraction at 2.98 Å resolution. Released 2 Mar 2016.
Explore 5EWL in 3D Show helices and sheets RCSB PDB PDBe
5EWL contains 70 α-helices and 72 β-strands across 4 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 | 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 | 93-95 | 3 | |
| α-helix | 105-114 | 10 | |
| β-strand | 118-120 | 3 | 1 |
| α-helix | 126-129 | 4 | |
| β-strand | 137-139 | 3 | 1 |
| α-helix | 144-147 | 4 | |
| α-helix | 148-158 | 11 | |
| β-strand | 162-168 | 7 | 2 |
| α-helix | 171-184 | 14 | |
| β-strand | 211-218 | 8 | 2 |
| α-helix | 226-233 | 8 | |
| β-strand | 239-243 | 5 | 2 |
| α-helix | 246-258 | 13 | |
| β-strand | 267-270 | 4 | 2 |
| α-helix | 273-275 | 3 | |
| α-helix | 278-282 | 5 | |
| α-helix | 283-284 | 2 | |
| β-strand | 288-292 | 5 | 2 |
| α-helix | 298-316 | 19 | |
| α-helix | 323-326 | 4 | |
| α-helix | 339-347 | 9 | |
| β-strand | 351-354 | 4 | 3 |
| β-strand | 357-359 | 3 | 3 |
| β-strand | 360-361 | 2 | 4 |
| β-strand | 366 | 1 | 1 |
| β-strand | 367-368 | 2 | 4 |
| 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 | 34-42 | 9 | 5 |
| α-helix | 47-50 | 4 | |
| β-strand | 65-73 | 9 | 5 |
| α-helix | 78-92 | 15 | |
| β-strand | 96-100 | 5 | 5 |
| α-helix | 107-119 | 13 | |
| β-strand | 123-127 | 5 | 5 |
| α-helix | 128-131 | 4 | |
| α-helix | 136-138 | 3 | |
| β-strand | 143-145 | 3 | 5 |
| α-helix | 150-164 | 15 | |
| β-strand | 168-173 | 6 | 6 |
| α-helix | 179-190 | 12 | |
| β-strand | 198-204 | 7 | 6 |
| α-helix | 215-220 | 6 | |
| β-strand | 227-231 | 5 | 6 |
| α-helix | 234-246 | 13 | |
| β-strand | 255-258 | 4 | 6 |
| α-helix | 260-263 | 4 | |
| α-helix | 274 | 1 | |
| β-strand | 278-282 | 5 | 6 |
| α-helix | 289-311 | 23 | |
| α-helix | 328-330 | 3 | |
| α-helix | 336-339 | 4 | |
| β-strand | 343-344 | 2 | 7 |
| β-strand | 347-348 | 2 | 7 |
| β-strand | 351 | 1 | 8 |
| β-strand | 356 | 1 | 5 |
| β-strand | 357 | 1 | 8 |
| β-strand | 362-367 | 6 | 6 |
| β-strand | 373-379 | 7 | 6 |
| β-strand | 384-386 | 3 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 25-33 | 9 | 9 |
| α-helix | 36-52 | 17 | |
| β-strand | 58-66 | 9 | 9 |
| 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 | 9 |
| α-helix | 105-114 | 10 | |
| β-strand | 118-120 | 3 | 9 |
| α-helix | 126-129 | 4 | |
| β-strand | 137-139 | 3 | 9 |
| α-helix | 144-147 | 4 | |
| α-helix | 148-158 | 11 | |
| β-strand | 162-168 | 7 | 10 |
| α-helix | 171-184 | 14 | |
| β-strand | 211-218 | 8 | 10 |
| α-helix | 226-233 | 8 | |
| β-strand | 239-243 | 5 | 10 |
| α-helix | 246-258 | 13 | |
| β-strand | 267-270 | 4 | 10 |
| α-helix | 273-275 | 3 | |
| α-helix | 278-282 | 5 | |
| α-helix | 283-284 | 2 | |
| β-strand | 288-292 | 5 | 10 |
| α-helix | 298-316 | 19 | |
| α-helix | 323-326 | 4 | |
| α-helix | 339-347 | 9 | |
| β-strand | 351-354 | 4 | 11 |
| β-strand | 357-359 | 3 | 11 |
| β-strand | 360-361 | 2 | 12 |
| β-strand | 366 | 1 | 9 |
| β-strand | 367-368 | 2 | 12 |
| β-strand | 372-378 | 7 | 10 |
| β-strand | 381-388 | 8 | 10 |
| β-strand | 393-395 | 3 | 10 |
| α-helix | 399-401 | 3 | |
| β-strand | 402 | 1 | 13 |
| β-strand | 406 | 1 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 34-42 | 9 | 14 |
| α-helix | 47-50 | 4 | |
| β-strand | 65-73 | 9 | 14 |
| α-helix | 78-91 | 14 | |
| β-strand | 96-100 | 5 | 14 |
| α-helix | 107-119 | 13 | |
| β-strand | 123-127 | 5 | 14 |
| α-helix | 128-131 | 4 | |
| α-helix | 136-138 | 3 | |
| β-strand | 143-145 | 3 | 14 |
| α-helix | 150-164 | 15 | |
| β-strand | 168-173 | 6 | 15 |
| α-helix | 179-191 | 13 | |
| β-strand | 198-204 | 7 | 15 |
| α-helix | 215-220 | 6 | |
| β-strand | 227-231 | 5 | 15 |
| α-helix | 234-246 | 13 | |
| β-strand | 255-258 | 4 | 15 |
| α-helix | 260-263 | 4 | |
| α-helix | 274 | 1 | |
| β-strand | 278-282 | 5 | 15 |
| α-helix | 289-311 | 23 | |
| α-helix | 324-330 | 7 | |
| α-helix | 336-339 | 4 | |
| α-helix | 350 | 1 | |
| β-strand | 351 | 1 | 16 |
| α-helix | 352 | 1 | |
| β-strand | 356 | 1 | 14 |
| β-strand | 357 | 1 | 16 |
| β-strand | 362-367 | 6 | 15 |
| β-strand | 373-379 | 7 | 15 |
| β-strand | 384-386 | 3 | 15 |
| α-helix | 391-393 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| NMDA glutamate receptor subunit | A, C | protein | 390 | Xenopus laevis | A0A1L8F5J9 (AlphaFold model) |
| Glutamate receptor ionotropic, NMDA 2B | B, D | protein | 364 | Homo sapiens | Q13224 (AlphaFold model) |
>5EWL_1 NMDA glutamate receptor subunit (chains A, C) DPKIVNIGAVLSTKKHEQIFREAVNQANKRHFTRKIQLQATSVTHRPNAIQMALSVCEDL ISSQVYAILVSHPPAPTDHLTPTPISYTAGFYRIPVIGLTTRMSIYSDKSIHLSFLRTVP PYSHQALVWFEMMRLFNWNHVILIVSDDHEGRAAQKKLETLLEGKESKSKKRNYENLDQL SYDNKRGPKADKVLQFEPGTKNLTALLLEAKELEARVIILSASEDDATAVYKSAAMLDMT GAGYVWLVGEREISGSALRYAPDGIIGLQLINGKNESAHISDAVAVVAQAIHELFEMENI TDPPRGCVGNTNIWKTGPLFKRVLMSSKYPDGVTGRIEFNEDGDRKFAQYSIMNLQNRKL VQVGIFNGSYIIQNDRKIIWPGGETELVPR
>5EWL_2 Glutamate receptor ionotropic, NMDA 2B (chains B, D) SPPSIGIAVILVGTSDEVAIKDAHEKDDFHHLSVVPRVELVAMNETDPKSIITRICDLMS DRKIQGVVFADDTDQEAIAQILDFISAQTLTPILGIHGGSSMIMADKDESSMFFQFGPSI EQQASVMLNIMEEYDWYIFSIVTTYFPGYQDFVNKIRSTIENSFVGWELEEVLLLDMSLD DGDSKIQNQLKKLQSPIILLYCTKEEATYIFEVANSVGLTGYGYTWIVPSLVAGDTDTVP AEFPTGLISVSYDEWDYGLPARVRDGIAIITTAASDMLSEHSFIPEPKSSCYNTHEKRIY QSNMLNRYLINVTFEGRDLSFSEDGYQMHPKLVIILLNKERKWERVGKWKDKSLQMKYYV WPRM
| ID | Name | Formula | Copies |
|---|---|---|---|
| 5SL | ~{N}-[(1~{S},3~{S})-3-[3-[(4-methylphenyl)methyl]-1,2,4-oxadiazol-5-yl]cyclopen… | C20 H21 N7 O | 2 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 6 |
Water and common crystallization additives (NA) are not listed.
A Novel Binding Mode Reveals Two Distinct Classes of NMDA Receptor GluN2B-selective Antagonists. Stroebel, D., Buhl, D.L., Knafels, J.D. et al. Mol Pharmacol (2016) 89:541-551. DOI 10.1124/mol.115.103036 · 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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