P10321: HLA class I histocompatibility antigen, C alpha chain (HLA-C)

HLA class I histocompatibility antigen, C alpha chain (HLA-C) is a 366-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P10321.

Gene
HLA-C
Organism
Homo sapiens
Length
366 residues
Mean pLDDT
86.4
Model
AF-P10321-F1 v6
Model created
1 Aug 2025
PDB structures
13

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Model confidence (pLDDT)

The mean pLDDT of this model is 86.4 (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 accurate74%
70 to 90Confident: backbone generally right8%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions14%

What pLDDT means and how to read it

Function

Antigen-presenting major histocompatibility complex class I (MHCI) molecule with an important role in reproduction and antiviral immunity (PubMed:11172028, PubMed:20104487, PubMed:20439706, PubMed:20972337, PubMed:24091323, PubMed:28649982, PubMed:29312307). In complex with B2M/beta 2 microglobulin displays a restricted repertoire of self and viral peptides and acts as a dominant ligand for inhibitory and activating killer immunoglobulin receptors (KIRs) expressed on NK cells (PubMed:16141329). In an allogeneic setting, such as during pregnancy, mediates interaction of extravillous trophoblasts with KIR on uterine NK cells and regulate trophoblast invasion necessary for placentation and…

Subunit structure

Heterotrimer that consists of an alpha chain HLA-C, a beta chain B2M and a peptide (peptide-HLA-C-B2M) (PubMed:10850706, PubMed:24990997, PubMed:28649982). Early in biogenesis, HLA-C-B2M dimer interacts with the components of the peptide-loading complex composed of TAPBP, TAP1-TAP2, TAPBPL, PDIA3/ERP57 and CALR (PubMed:18420581). Interacts with TAP1-TAP2 transporter via TAPBP; this interaction…

Subcellular location

Cell membrane, Endoplasmic reticulum membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6JTOX-ray1.7 ÅA=26-298
5W6AX-ray1.74 ÅA/C=25-300
4NT6X-ray1.84 ÅA=26-298
5W67X-ray2.3 ÅA=25-300
5VGDX-ray2.32 ÅA=26-302
3BZFX-ray2.5 ÅP/Q=3-11
6PAGX-ray2.5 ÅA=25-302
5VGEX-ray2.6 ÅA=26-300
1QQDX-ray2.7 ÅA=26-298
1IM9X-ray2.8 ÅA/E=26-299
5W69X-ray2.8 ÅA/C/E/G=25-300
1EFXX-ray3.0 ÅA=26-302
6PA1X-ray3.01 ÅA/E=25-301

More AlphaFold highlights

About this viewer

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