O15399: Glutamate receptor ionotropic, NMDA 2D (GRIN2D)

Glutamate receptor ionotropic, NMDA 2D (GRIN2D) is a 1336-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O15399.

Gene
GRIN2D
Organism
Homo sapiens
Length
1336 residues
Mean pLDDT
63.2
Model
AF-O15399-F1 v6
Model created
1 Aug 2025
PDB structures
13

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Model confidence (pLDDT)

The mean pLDDT of this model is 63.2 (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 accurate15%
70 to 90Confident: backbone generally right37%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions40%

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:26875626, PubMed:27616483, PubMed:28126851, PubMed:9489750). Participates in synaptic plasticity for learning and memory formation (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+) (PubMed:26875626, PubMed:27616483, PubMed:28126851, PubMed:9489750). NMDARs mediate simultaneously the potassium efflux and the influx…

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:26875626, PubMed:28126851, PubMed:36959261, PubMed:9489750). In vivo, the subunit composition may depend on the expression levels of the different subunits (Probable).…

Subcellular location

Cell membrane, Postsynaptic cell membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9D37EM3.34 ÅD=28-880
8E96EM3.38 ÅB/D=28-879
7YFFEM3.6 ÅB/D=1-879
9D39EM3.65 ÅD=28-880
9D3BEM3.71 ÅD=28-880
9D3AEM3.78 ÅD=28-880
7YFLEM3.9 ÅB/D=1-879
9D38EM3.95 ÅD=28-880
9D3CEM3.96 ÅD=28-880
8Y1VEM4.2 ÅB/D=1-879
7YFMEM5.1 ÅB/D=1-879
7YFREM5.1 ÅB/D=1-879
7YFOEM6.4 ÅB/D=1-879

More AlphaFold highlights

About this viewer

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