Crystal structure of amino terminal domains of the NMDA receptor subunit GluN1 and GluN2B in apo closed state. Determined by X-ray diffraction at 3.1 Å resolution. Released 14 Dec 2016.
Explore 5TPZ in 3D Show helices and sheets RCSB PDB PDBe
5TPZ contains 31 α-helices and 37 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 | 25-33 | 9 | 1 |
| α-helix | 36-52 | 17 | |
| β-strand | 58-62 | 5 | 1 |
| β-strand | 65-66 | 2 | 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 | 105-114 | 10 | |
| α-helix | 116-117 | 2 | |
| 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 | 163-168 | 6 | 2 |
| α-helix | 171-184 | 14 | |
| β-strand | 213-218 | 6 | 2 |
| α-helix | 226-235 | 10 | |
| β-strand | 239-243 | 5 | 2 |
| α-helix | 246-257 | 12 | |
| β-strand | 267-269 | 3 | 2 |
| α-helix | 273-275 | 3 | |
| α-helix | 280-282 | 3 | |
| α-helix | 284 | 1 | |
| β-strand | 287-292 | 6 | 2 |
| α-helix | 298-316 | 19 | |
| α-helix | 324-326 | 3 | |
| α-helix | 339-348 | 10 | |
| β-strand | 351 | 1 | 3 |
| β-strand | 359 | 1 | 3 |
| β-strand | 361 | 1 | 4 |
| β-strand | 367 | 1 | 4 |
| β-strand | 372-378 | 7 | 2 |
| β-strand | 381-388 | 8 | 2 |
| β-strand | 393-395 | 3 | 2 |
| α-helix | 399-400 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 34-42 | 9 | 5 |
| β-strand | 65-73 | 9 | 5 |
| α-helix | 78-90 | 13 | |
| β-strand | 97-101 | 5 | 5 |
| α-helix | 107-119 | 13 | |
| β-strand | 123-127 | 5 | 5 |
| α-helix | 128-131 | 4 | |
| β-strand | 143-145 | 3 | 5 |
| β-strand | 148 | 1 | 6 |
| α-helix | 150-163 | 14 | |
| β-strand | 168-173 | 6 | 7 |
| α-helix | 179-191 | 13 | |
| β-strand | 198-204 | 7 | 7 |
| α-helix | 215-220 | 6 | |
| β-strand | 227-231 | 5 | 7 |
| α-helix | 234-246 | 13 | |
| β-strand | 255-257 | 3 | 7 |
| β-strand | 258 | 1 | 8 |
| α-helix | 260-263 | 4 | |
| α-helix | 274 | 1 | |
| β-strand | 279-282 | 4 | 8 |
| α-helix | 289-311 | 23 | |
| α-helix | 329-339 | 11 | |
| β-strand | 343 | 1 | 9 |
| β-strand | 348 | 1 | 9 |
| β-strand | 351 | 1 | 6 |
| β-strand | 357 | 1 | 6 |
| β-strand | 362-367 | 6 | 8 |
| β-strand | 373-379 | 7 | 8 |
| β-strand | 384-386 | 3 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| NMDA glutamate receptor subunit | A | protein | 383 | Xenopus laevis | A0A1L8F5J9 (AlphaFold model) |
| Glutamate receptor ionotropic, NMDA 2B | D | protein | 362 | Rattus norvegicus | Q00960 (AlphaFold model) |
>5TPZ_1 NMDA glutamate receptor subunit (chains A) DPKIVNIGAVLSTKKHEQIFREAVNQANKRHFTRKIQLQATSVTHRPNAIQMALSVCEDL ISSQVYAILVSHPPAPTDHLTPTPISYTAGFYRIPVIGLTTRMSIYSDKSIHLSFLRTVP PYSHQALVWFEMMRLFNWNHVILIVSDDHEGRAAQKKLETLLEGKESKSKKRNYENLDQL SYDNKRGPKADKVLQFEPGTKNLTALLLEAKELEARVIILSASEDDATAVYKSAAMLDMT GAGYVWLVGEREISGSALRYAPDGIIGLQLINGKNESAHISDAVAVVAQAIHELFEMENI TDPPRGCVGNTNIWKTGPLFKRVLMSSKYPDGVTGRIEFNEDGDRKFAQYSIMNLQNRKL VQVGIFNGSYIIQNDRKIIWPGG
>5TPZ_2 Glutamate receptor ionotropic, NMDA 2B (chains D) PPSIGIAVILVGTSDEVAIKDAHEKDDFHHLSVVPRVELVAMNETDPKSIITRICDLMSD RKIQGVVFADDTDQEAIAQILDFISAQTLTPILGIHGGSSMIMADKDESSMFFQFGPSIE QQASVMLNIMEEYDWYIFSIVTTYFPGYQDFVNKIRSTIENSFVGWELEEVLLLDMSLDD GDSKIQNQLKKLQSPIILLYCTKEEATYIFEVANSVGLTGYGYTWIVPSLVAGDTDTVPS EFPTGLISVSYDEWDYGLPARVRDGIAIITTAASDMLSEHSFIPEPKSSCYNTHEKRIYQ SNMLNRYLINVTFEGRDLSFSEDGYQMHPKLVIILLNKERKWERVGKWKDKSLQMKYYVW PR
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 4 |
Molecular Basis for Subtype Specificity and High-Affinity Zinc Inhibition in the GluN1-GluN2A NMDA Receptor Amino-Terminal Domain. Romero-Hernandez, A., Simorowski, N., Karakas, E. et al. Neuron (2016) 92:1324-1336. DOI 10.1016/j.neuron.2016.11.006 · 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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