Crystal structure of the NR1 ligand-binding core in complex with ACPC. Determined by X-ray diffraction at 1.4 Å resolution. Released 12 Jul 2005.
Explore 1Y20 in 3D Show helices and sheets RCSB PDB PDBe
1Y20 contains 14 α-helices and 23 β-strands across 1 chain. 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 | 6-10 | 5 | 1 |
| β-strand | 13 | 1 | 2 |
| β-strand | 17 | 1 | 2 |
| β-strand | 18-21 | 4 | 1 |
| β-strand | 32 | 1 | 3 |
| α-helix | 37 | 1 | |
| β-strand | 38 | 1 | 3 |
| α-helix | 39-40 | 2 | |
| β-strand | 42-47 | 6 | 1 |
| β-strand | 58-64 | 7 | 1 |
| α-helix | 66-77 | 12 | |
| β-strand | 82-86 | 5 | 1 |
| β-strand | 95-97 | 3 | 4 |
| β-strand | 104-106 | 3 | 4 |
| α-helix | 108-115 | 8 | |
| β-strand | 120-121 | 2 | 1 |
| α-helix | 125 | 1 | |
| β-strand | 126 | 1 | 5 |
| α-helix | 127 | 1 | |
| α-helix | 129-132 | 4 | |
| β-strand | 135-137 | 3 | 1 |
| β-strand | 142-151 | 10 | 5 |
| α-helix | 162-165 | 4 | |
| β-strand | 168 | 1 | 6 |
| β-strand | 171 | 1 | 6 |
| β-strand | 173-174 | 2 | 5 |
| β-strand | 176 | 1 | 7 |
| α-helix | 180-185 | 6 | |
| α-helix | 189-199 | 11 | |
| β-strand | 203 | 1 | 7 |
| α-helix | 206-214 | 9 | |
| β-strand | 220-224 | 5 | 5 |
| α-helix | 225-234 | 10 | |
| β-strand | 238-250 | 13 | 5 |
| β-strand | 253-255 | 3 | 1 |
| α-helix | 261-273 | 13 | |
| α-helix | 276-284 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glutamate [NMDA] receptor subunit zeta 1 | A | protein | 292 | Rattus norvegicus | P35439 (AlphaFold model) |
>1Y20_1 Glutamate [NMDA] receptor subunit zeta 1 (chains A) GMSTRLKIVTIHQEPFVYVKPTMSDGTCKEEFTVNGDPVKKVICTGPNDTSPGSPRHTVP QCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADM IVAPLTINNERAQYIEFSKPFKYQGLTILVKKGTRITGINDPRLRNPSDKFIYATVKQSS VDIYFRRQVELSTMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVT TGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRYQECDS
| ID | Name | Formula | Copies |
|---|---|---|---|
| 1AC | 1-aminocyclopropanecarboxylic acid | C4 H7 N O2 | 1 |
Mechanism of Partial Agonist Action at the NR1 Subunit of NMDA Receptors. Inanobe, A., Furukawa, H., Gouaux, E. Neuron (2005) 47:71-84. DOI 10.1016/j.neuron.2005.05.022 · PubMed
Other PDB entries of the same protein (UniProt P35439 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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