B7ZSK1: Glutamate receptor ionotropic, NMDA 2A (grin2a)

Glutamate receptor ionotropic, NMDA 2A (grin2a) is a 1451-residue protein from Xenopus laevis. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: B7ZSK1.

Gene
grin2a
Organism
Xenopus laevis
Length
1451 residues
Mean pLDDT
61.3
Model
AF-B7ZSK1-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 61.3 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate19%
70 to 90Confident: backbone generally right29%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions42%

What pLDDT means and how to read it

Function

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:28232581). MDARs 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:28232581). NMDARs mediate simultaneously the potassium efflux and the influx of calcium and sodium (By similarity). Each GluN2 subunit confers differential attributes to channel properties, including activation,…

Subunit structure

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:28232581). In vivo, the subunit composition may depend on the expression levels of the different subunits (Probable)

Subcellular location

Cell membrane, Postsynaptic cell membrane

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
5UOWEM4.5 ÅB=1-834
5UP2EM6.0 ÅB=1-834

More AlphaFold highlights

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