Crystal structure of GluN1/GluN2A ligand-binding domain in complex with Compound 1, Glycine and Glutamate. Determined by X-ray diffraction at 2.4 Å resolution. Released 5 Mar 2025.
Explore 9MUL in 3D Show helices and sheets RCSB PDB PDBe
9MUL contains 31 α-helices and 39 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 | 398-402 | 5 | 1 |
| β-strand | 405 | 1 | 2 |
| β-strand | 409 | 1 | 2 |
| β-strand | 410-413 | 4 | 1 |
| β-strand | 424 | 1 | 3 |
| α-helix | 429 | 1 | |
| β-strand | 430 | 1 | 3 |
| α-helix | 431-432 | 2 | |
| β-strand | 434-439 | 6 | 1 |
| β-strand | 450-456 | 7 | 1 |
| α-helix | 458-470 | 13 | |
| β-strand | 474-478 | 5 | 1 |
| β-strand | 487 | 1 | 4 |
| β-strand | 498 | 1 | 4 |
| α-helix | 500-507 | 8 | |
| β-strand | 512-513 | 2 | 1 |
| β-strand | 518 | 1 | 5 |
| α-helix | 521-524 | 4 | |
| β-strand | 528-529 | 2 | 1 |
| α-helix | 530 | 1 | |
| α-helix | 532 | 1 | |
| β-strand | 534-543 | 10 | 5 |
| α-helix | 670-673 | 4 | |
| β-strand | 681-682 | 2 | 5 |
| β-strand | 684 | 1 | 6 |
| α-helix | 688-695 | 8 | |
| α-helix | 697-699 | 3 | |
| α-helix | 700-706 | 7 | |
| β-strand | 711 | 1 | 6 |
| α-helix | 714-722 | 9 | |
| β-strand | 728-732 | 5 | 5 |
| α-helix | 733-742 | 10 | |
| β-strand | 746-758 | 13 | 5 |
| β-strand | 761-762 | 2 | 1 |
| α-helix | 769-781 | 13 | |
| α-helix | 784-788 | 5 | |
| α-helix | 789-793 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 405-410 | 6 | 7 |
| β-strand | 413 | 1 | 8 |
| β-strand | 417 | 1 | 8 |
| β-strand | 418-420 | 3 | 7 |
| β-strand | 434-441 | 8 | 7 |
| β-strand | 449-457 | 9 | 7 |
| α-helix | 459-470 | 12 | |
| β-strand | 474-479 | 6 | 7 |
| β-strand | 488-489 | 2 | 9 |
| β-strand | 492-493 | 2 | 9 |
| α-helix | 495-501 | 7 | |
| β-strand | 507-508 | 2 | 7 |
| β-strand | 513 | 1 | 10 |
| α-helix | 516-519 | 4 | |
| β-strand | 523-524 | 2 | 7 |
| β-strand | 529-538 | 10 | 10 |
| α-helix | 668-671 | 4 | |
| α-helix | 673-675 | 3 | |
| α-helix | 679-681 | 3 | |
| β-strand | 682-683 | 2 | 10 |
| α-helix | 689-697 | 9 | |
| α-helix | 699-705 | 7 | |
| α-helix | 706-708 | 3 | |
| α-helix | 713-721 | 9 | |
| β-strand | 727-731 | 5 | 10 |
| α-helix | 732-740 | 9 | |
| α-helix | 743-745 | 3 | |
| β-strand | 747-749 | 3 | 10 |
| α-helix | 750-753 | 4 | |
| β-strand | 756-761 | 6 | 10 |
| β-strand | 764-765 | 2 | 7 |
| α-helix | 772-784 | 13 | |
| α-helix | 787-795 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glutamate receptor ionotropic, NMDA 1 | A | protein | 306 | Homo sapiens | Q05586 (AlphaFold model) |
| Glutamate receptor ionotropic, NMDA 2A | B | protein | 297 | Homo sapiens | Q12879 (AlphaFold model) |
>9MUL_1 Glutamate receptor ionotropic, NMDA 1 (chains A) MHHHHHHENLYFQGSMSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGDPVKKVICTG PNDTSPGSPRHTVPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEW NGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKGTRITGINDPRLRN PSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSA VLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVR YQECDS
>9MUL_2 Glutamate receptor ionotropic, NMDA 2A (chains B) MHHHHHHENLYFQGPDDNHLSIVTLEEAPFVIVEDIDPLTETCVRNTVPCRKFVKINNST NEGMNVKKCCKGFCIDILKKLSRTVKFTYDLYLVTNGKHGKKVNNVWNGMIGEVVYQRAV MAVGSLTINEERSEVVDFSVPFVETGISVMVSRGTQVTGLSDKKFQRPHDYSPPFRFGTV PNGSTERNIRNNYPYMHQYMTKFNQKGVEDALVSLKTGKLDAFIYDAAVLNYKAGRDEGC KLVTIGSGYIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLWLTGICHN
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1BRA | 5-[(3-chlorobenzene-1-sulfonyl)methoxy]-6-methyl-N-[(pyridin-3-yl)methyl]pyrazi… | C19 H17 Cl N4 O4 S | 1 |
| GLU | Glutamic acid | C5 H9 N O4 | 1 |
| GLY | Glycine | C2 H5 N O2 | 1 |
Design, Synthesis, and Characterization of GluN2A Negative Allosteric Modulators Suitable for In Vivo Exploration. Bischoff, F.P., Van Brandt, S., Viellevoye, M. et al. J Med Chem (2025) 68:4672-4693. DOI 10.1021/acs.jmedchem.4c02751 · PubMed
Other PDB entries of the same protein (UniProt Q05586 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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