Q9NZQ7: Programmed cell death 1 ligand 1 (CD274)

Programmed cell death 1 ligand 1 (CD274) is a 290-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9NZQ7.

Gene
CD274
Organism
Homo sapiens
Length
290 residues
Mean pLDDT
88.3
Model
AF-Q9NZQ7-F1 v6
Model created
1 Aug 2025
PDB structures
74

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Model confidence (pLDDT)

The mean pLDDT of this model is 88.3 (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 accurate71%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution14%
Below 50Very low: often disordered regions2%

What pLDDT means and how to read it

Function

Plays a critical role in induction and maintenance of immune tolerance to self (PubMed:11015443, PubMed:28813410, PubMed:28813417, PubMed:31399419). As a ligand for the inhibitory receptor PDCD1/PD-1, modulates the activation threshold of T-cells and limits T-cell effector response (PubMed:11015443, PubMed:28813410, PubMed:28813417, PubMed:36727298). Through a yet unknown activating receptor, may costimulate T-cell subsets that predominantly produce interleukin-10 (IL10) (PubMed:10581077). Can also act as a transcription coactivator: in response to hypoxia, translocates into the nucleus via its interaction with phosphorylated STAT3 and promotes transcription of GSDMC, leading to pyroptosis…

Subunit structure

Interacts with PDCD1 (PubMed:11015443, PubMed:18287011, PubMed:26602187). Interacts (via transmembrane domain) with CMTM4 and CMTM6 (PubMed:28813410, PubMed:28813417). Interacts with (phosphorylated) STAT3; promoting nuclear translocation (PubMed:32929201). Interacts with CD80 (PubMed:36727298)

Subcellular location

Cell membrane, Early endosome membrane, Recycling endosome membrane, Nucleus, Endomembrane system, Secreted

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5O45X-ray0.99 ÅA=17-134
8ALXX-ray1.1 ÅA=18-134
6NP9X-ray1.27 ÅA=18-134
9I0UX-ray1.46 ÅA/B=18-134
6YCRX-ray1.54 ÅA=18-134
8AOKX-ray1.6 ÅA=18-134
7CZDX-ray1.64 ÅB/D=19-134
5JDSX-ray1.7 ÅA=18-132
5N2FX-ray1.7 ÅA/B=18-134
9QSMX-ray1.75 ÅA/B/C/D/E/F=18-134
8ZNLX-ray1.77 ÅB/D/F/H=19-132
5C3TX-ray1.8 ÅA=18-134
7OUNX-ray1.9 ÅA=17-134
6NNVX-ray1.92 ÅA/B/C/D=18-134
4Z18X-ray1.95 ÅA/B=19-239
8XR5X-ray1.95 ÅA/B=19-134
6PV9X-ray2.0 ÅA=19-239
7C88X-ray2.0 ÅC/M=1-136
7SJQX-ray2.0 ÅA=18-134
5NIUX-ray2.01 ÅA/B/C/D=18-134

Showing 20 of 74 experimental structures (best resolution first).

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