Glutamate receptor ionotropic, NMDA 2B (Grin2b) is a 1482-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q00960.
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The mean pLDDT of this model is 60.7 (low 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 | 18% |
| 70 to 90 | Confident: backbone generally right | 30% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 44% |
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:11929923, PubMed:19910922, PubMed:21677647, PubMed:24607230, PubMed:24876489, PubMed:27135925, PubMed:7524561). Participates in synaptic plasticity for learning and memory formation by contributing to the long-term depression (LTD) of hippocampus membrane currents (By similarity). Channel activation requires binding of the neurotransmitter L-glutamate to the GluN2 subunit, glycine or D-serine binding to the GluN1 subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+)…
Heterotetramer. 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) (PubMed:1350383, PubMed:19910922, PubMed:21677647, PubMed:24876489, PubMed:27135925, PubMed:27916457). Can also form heterotetrameric channels that contain at least two GluN1…
Cell membrane, Postsynaptic cell membrane, Late endosome, Lysosome, Cytoplasm, cytoskeleton
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6E7R | X-ray | 2.1 Å | B/D=32-394 |
| 6E7U | X-ray | 2.27 Å | B/D=32-394 |
| 6E7T | X-ray | 2.31 Å | B/D=32-393 |
| 6E7X | X-ray | 2.58 Å | B/D=32-394 |
| 9OBX | EM | 2.59 Å | B/D=27-852 |
| 3QEL | X-ray | 2.6 Å | B/D=31-394 |
| 6E7V | X-ray | 2.6 Å | B/D=32-394 |
| 6E7W | X-ray | 2.67 Å | B/D=32-394 |
| 9OC2 | EM | 2.69 Å | B/D=27-852 |
| 6E7S | X-ray | 2.72 Å | B/D=32-394 |
| 9OC1 | EM | 2.76 Å | B/D=27-852 |
| 3JPW | X-ray | 2.8 Å | A=32-394 |
| 9OBZ | EM | 2.81 Å | B/D=27-852 |
| 8G18 | X-ray | 2.85 Å | B/D=32-394 |
| 5B3J | X-ray | 2.9 Å | C/D=31-394 |
| 7SAA | EM | 2.97 Å | B/D=27-852 |
| 9OC0 | EM | 2.97 Å | B/D=27-852 |
| 3QEM | X-ray | 3.0 Å | B/D=31-394 |
| 9OBT | EM | 3.01 Å | B/D=27-852 |
| 5TPZ | X-ray | 3.1 Å | D=32-393 |
Showing 20 of 64 experimental structures (best resolution first).
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