Glutamate receptor ionotropic, NMDA 1 (grin1) is a 903-residue protein from Xenopus laevis. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: A0A1L8F5J9.
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The mean pLDDT of this model is 85.3 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.
| pLDDT band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 58% |
| 70 to 90 | Confident: backbone generally right | 29% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 6% |
What pLDDT means and how to read it
Component of N-methyl-D-aspartate (NMDA) receptors (NMDARs) that function as heterotetrameric, ligand-gated cation channels with high calcium permeability and voltage-dependent block by Mg(2+) (PubMed:16214956, PubMed:19524674). NMDARs participate in synaptic plasticity (By similarity). Channel activation requires binding of the neurotransmitter L-glutamate to the GluN2 subunit, glycine binding to the GluN1 subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+) (PubMed:16214956, PubMed:19524674, PubMed:21677647, PubMed:25008524, PubMed:26912815, PubMed:27135925, PubMed:27916457, PubMed:28232581). NMDARs mediate simultaneously the potassium efflux and the influx of…
Heterotetramer; the NMDAR subunits are modular and harbor tiered domains that function in concert to regulate opening and closing of the cation-selective ion channel pore (PubMed:27062927). Forms heterotetrameric channels composed of two GluN1/zeta subunits (GRIN1), and two identical GluN2/epsilon subunits (GRIN2A, GRIN2B, GRIN2C or GRIN2D) or GluN3 subunits (GRIN3A or GRIN3B) (in vitro)…
Cell membrane, Postsynaptic cell membrane, Postsynaptic density membrane, Synaptic cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3QEK | X-ray | 2.0 Å | A/B=23-384 |
| 6E7R | X-ray | 2.1 Å | A/C=23-386 |
| 6E7U | X-ray | 2.27 Å | A/C=23-386 |
| 6E7T | X-ray | 2.31 Å | A/C=23-386 |
| 6E7X | X-ray | 2.58 Å | A/C=23-386 |
| 3QEL | X-ray | 2.6 Å | A/C=23-384 |
| 6E7V | X-ray | 2.6 Å | A/C=23-386 |
| 6E7W | X-ray | 2.67 Å | A/C=23-386 |
| 5TQ0 | X-ray | 2.7 Å | A=24-387 |
| 6E7S | X-ray | 2.72 Å | A/C=23-386 |
| 5EWM | X-ray | 2.76 Å | A/C=23-387 |
| 5EWJ | X-ray | 2.77 Å | A/C=23-387 |
| 5B3J | X-ray | 2.9 Å | A/B=23-384 |
| 5TPW | X-ray | 2.91 Å | A=24-387 |
| 5EWL | X-ray | 2.98 Å | A/C=23-387 |
| 3QEM | X-ray | 3.0 Å | A/C=23-384 |
| 5TPZ | X-ray | 3.1 Å | A=23-384 |
| 5TQ2 | X-ray | 3.29 Å | A=24-387 |
| 4TLL | X-ray | 3.59 Å | A/C=22-836 |
| 5UN1 | X-ray | 3.6 Å | A/C/E/G=394-836 |
Showing 20 of 32 experimental structures (best resolution first).
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