Q13241: Natural killer cells antigen CD94 (KLRD1)

Natural killer cells antigen CD94 (KLRD1) is a 179-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13241.

Gene
KLRD1
Organism
Homo sapiens
Length
179 residues
Mean pLDDT
87.6
Model
AF-Q13241-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 87.6 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate72%
70 to 90Confident: backbone generally right12%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions7%

What pLDDT means and how to read it

Function

Immune receptor involved in self-nonself discrimination. In complex with KLRC1 or KLRC2 on cytotoxic and regulatory lymphocyte subsets, recognizes non-classical major histocompatibility (MHC) class Ib molecule HLA-E loaded with self-peptides derived from the signal sequence of classical MHC class Ia and non-classical MHC class Ib molecules (PubMed:10023772, PubMed:18064301, PubMed:18083576, PubMed:37264229, PubMed:9486650, PubMed:9754572). Enables cytotoxic cells to monitor the expression of MHC class I molecules in healthy cells and to tolerate self (PubMed:12387742, PubMed:18064301, PubMed:9430220). Primarily functions as a ligand binding subunit as it lacks the capacity to signal

Subunit structure

Can form disulfide-bonded heterodimer with NKG2 family members KLRC1 and KLRC2 (PubMed:18083576, PubMed:18332182, PubMed:18448674, PubMed:9655483). KLRD1-KLRC1 heterodimer interacts with peptide-bound HLA-E-B2M heterotrimeric complex. KLRD1 plays a prominent role in directly interacting with HLA-E (PubMed:18083576). KLRD1-KLRC1 interacts with much higher affinity with peptide-bound HLA-E-B2M…

Subcellular location

Cell membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3BDWX-ray2.5 ÅA/C=57-179
1B6EX-ray2.6 ÅA=52-179
3CDGX-ray3.4 ÅE/J=57-179
3CIIX-ray4.41 ÅG/I=59-179

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