P01889: HLA class I histocompatibility antigen, B alpha chain (HLA-B)

HLA class I histocompatibility antigen, B alpha chain (HLA-B) is a 362-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P01889.

Gene
HLA-B
Organism
Homo sapiens
Length
362 residues
Mean pLDDT
88.1
Model
AF-P01889-F1 v6
Model created
1 Aug 2025
PDB structures
237

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Model confidence (pLDDT)

The mean pLDDT of this model is 88.1 (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 accurate78%
70 to 90Confident: backbone generally right6%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions12%

What pLDDT means and how to read it

Function

Antigen-presenting major histocompatibility complex class I (MHCI) molecule. In complex with B2M/beta 2 microglobulin displays primarily viral and tumor-derived peptides on antigen-presenting cells for recognition by alpha-beta T cell receptor (TCR) on HLA-B-restricted CD8-positive T cells, guiding antigen-specific T cell immune response to eliminate infected or transformed cells (PubMed:23209413, PubMed:25808313, PubMed:29531227, PubMed:9620674). May also present self-peptides derived from the signal sequence of secreted or membrane proteins, although T cells specific for these peptides are usually inactivated to prevent autoreactivity (PubMed:18991276, PubMed:7743181). Both the peptide…

Subunit structure

Heterotrimer that consists of an alpha chain HLA-B, a beta chain B2M and a peptide (peptide-HLA-B-B2M) (PubMed:15657948, PubMed:17057332, PubMed:22020283, PubMed:24600035, PubMed:25808313, PubMed:29531227). Early in biogenesis, HLA-B-B2M dimer interacts with the components of the peptide-loading complex composed of TAPBP, TAP1-TAP2, TAPBPL, PDIA3/ERP57 and CALR (PubMed:26416272, PubMed:26439010,…

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
1K5NX-ray1.09 ÅA=25-300
4U1MX-ray1.18 ÅA=25-301
3CZFX-ray1.2 ÅA=25-300
6MT3X-ray1.21 ÅA=25-300
3BWAX-ray1.3 ÅA=25-300
3LN4X-ray1.3 ÅA=25-298
3SPVX-ray1.3 ÅA=25-300
6MT6X-ray1.31 ÅA=25-300
2BVPX-ray1.35 ÅA=25-300
6MTLX-ray1.35 ÅA=25-300
4U1JX-ray1.38 ÅA=25-301
6PYWX-ray1.38 ÅA=25-300
2A83X-ray1.4 ÅA=25-300
4QRSX-ray1.4 ÅA=25-300
4QRTX-ray1.4 ÅA=25-300
5WMQX-ray1.4 ÅA=25-300
6P2CX-ray1.4 ÅA=25-300
4XXCX-ray1.43 ÅA=25-303
5IB2X-ray1.44 ÅA=25-300
6PYJX-ray1.44 ÅA=25-300

Showing 20 of 237 experimental structures (best resolution first).

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