CD44 antigen (Cd44) is a 778-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P15379.
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The mean pLDDT of this model is 52.4 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 20% |
| 70 to 90 | Confident: backbone generally right | 4% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 70% |
What pLDDT means and how to read it
Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment. Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, inflammation and response to bacterial infection. Engages, through its ectodomain, extracellular matrix components such as hyaluronan/HA, collagen, growth factors, cytokines or proteases and serves as a platform for signal transduction by assembling, via its cytoplasmic domain, protein complexes containing receptor kinases and membrane proteases (PubMed:25065622,…
Interacts with PKN2 (PubMed:17403031). Interacts with TIAM1 and TIAM2 (PubMed:19893486). Interacts with HA, as well as other glycosaminoglycans, collagen, laminin, and fibronectin via its N-terminal segment (PubMed:24606063). Interacts with UNC119. Interacts with PDPN (via extracellular domain); this interaction is required for PDPN-mediated directional migration and regulation of lamellipodia…
Cell membrane, Cell projection, microvillus, Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5SBQ | X-ray | 0.99 Å | A=23-172 |
| 5SBS | X-ray | 1.02 Å | A=23-172 |
| 5SBU | X-ray | 1.04 Å | A=23-172 |
| 5SBX | X-ray | 1.05 Å | A=23-172 |
| 5SBV | X-ray | 1.11 Å | A=23-172 |
| 4MRH | X-ray | 1.12 Å | A=23-171 |
| 5SBM | X-ray | 1.14 Å | A=23-172 |
| 5BZR | X-ray | 1.15 Å | A=21-171 |
| 5SBW | X-ray | 1.15 Å | A=23-172 |
| 5SBT | X-ray | 1.16 Å | A=23-172 |
| 5SBZ | X-ray | 1.17 Å | A=23-172 |
| 5SC1 | X-ray | 1.17 Å | A=23-172 |
| 5SC4 | X-ray | 1.17 Å | A=23-172 |
| 5SC5 | X-ray | 1.17 Å | A=23-172 |
| 5SBN | X-ray | 1.18 Å | A=23-172 |
| 5SC0 | X-ray | 1.19 Å | A=23-172 |
| 5BZQ | X-ray | 1.2 Å | A=21-171 |
| 5SBL | X-ray | 1.2 Å | A=23-172 |
| 5SC7 | X-ray | 1.2 Å | A=23-172 |
| 5SC2 | X-ray | 1.21 Å | A=23-172 |
Showing 20 of 53 experimental structures (best resolution first).
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