A7XY94: Glutamate receptor ionotropic, NMDA 2B (grin2b)

Glutamate receptor ionotropic, NMDA 2B (grin2b) is a 1448-residue protein from Xenopus laevis. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: A7XY94.

Gene
grin2b
Organism
Xenopus laevis
Length
1448 residues
Mean pLDDT
62.1
Model
AF-A7XY94-F1 v6
Model created
1 Aug 2025
PDB structures
13

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Model confidence (pLDDT)

The mean pLDDT of this model is 62.1 (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 accurate21%
70 to 90Confident: backbone generally right28%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions41%

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:18177891, PubMed:25008524, PubMed:28232581). 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:18177891, PubMed:25008524, 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…

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:18177891, PubMed:25008524, PubMed:27062927, 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
4TLLX-ray3.59 ÅB/D=20-839
5UN1X-ray3.6 ÅB/D/F/H=400-839
4TLMX-ray3.77 ÅB/D=20-839
5UOWEM4.5 ÅD=1-840
5UP2EM6.0 ÅD=1-840
5IOUEM7.0 ÅB/D=1-839
5IOVEM7.5 ÅB/D=1-839
5IPVEM9.25 ÅB/D=1-839
5IPQEM13.5 ÅB/D=1-839
5IPSEM13.5 ÅB/D=1-839
5IPREM14.1 ÅB/D=1-839
5IPTEM14.1 ÅB/D=1-839
5IPUEM15.4 ÅB/D=1-839

More AlphaFold highlights

About this viewer

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