C-X-C chemokine receptor type 4 (CXCR4) is a 352-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P61073.
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The mean pLDDT of this model is 82.3 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 57% |
| 70 to 90 | Confident: backbone generally right | 22% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 13% |
What pLDDT means and how to read it
Receptor for the C-X-C chemokine CXCL12/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1/MAPK3 activation (PubMed:10074102, PubMed:10452968, PubMed:10644702, PubMed:10825158, PubMed:18799424, PubMed:20048153, PubMed:20505072, PubMed:24912431, PubMed:28978524, PubMed:8752280, PubMed:8752281). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase (PubMed:16725153, PubMed:17197449, PubMed:18799424, PubMed:39093700). CXCR4 is coupled to G(i) G alpha proteins and mediates inhibition of adenylate cyclase…
Monomer. Can form homodimers (PubMed:20929726). Interacts with CD164 (PubMed:17077324). Interacts (when phosphorylated) with ARRB1; the interaction is associated with internalization of the receptor and short-term desensitization to the ligand (PubMed:37209686). Interacts with ARRB2; the interaction is dependent on the C-terminal phosphorylation of CXCR4 and allows activation of MAPK1 and MAPK3.…
Cell membrane, Cell junction, Early endosome, Late endosome, Lysosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3ODU | X-ray | 2.5 Å | A/B=2-319 |
| 9UPV | EM | 2.7 Å | R=1-337 |
| 8U4N | EM | 2.72 Å | R=2-352 |
| 9UPU | EM | 2.8 Å | R=1-337 |
| 8K3Z | EM | 2.81 Å | A=25-320 |
| 3OE0 | X-ray | 2.9 Å | A=2-319 |
| 9MDU | EM | 2.9 Å | A/B/C/D=1-352 |
| 8YU7 | EM | 3.01 Å | A/B/C/D=2-352 |
| 8ZPL | EM | 3.01 Å | R=1-224, R=241-319 |
| 3OE8 | X-ray | 3.1 Å | A/B/C=2-319 |
| 3OE9 | X-ray | 3.1 Å | A/B=2-319 |
| 4RWS | X-ray | 3.1 Å | A=2-228, A=231-319 |
| 8U4R | EM | 3.1 Å | R=2-352 |
| 8U4P | EM | 3.15 Å | R=2-352 |
| 3OE6 | X-ray | 3.2 Å | A=2-325 |
| 8ZPM | EM | 3.2 Å | R=1-224, R=241-319 |
| 22XC | EM | 3.28 Å | C/G/R=2-352 |
| 8U4O | EM | 3.29 Å | R=2-352 |
| 8ZPN | EM | 3.31 Å | R=1-224, R=241-319 |
| 8U4S | EM | 3.35 Å | C/G/R=2-352 |
Showing 20 of 33 experimental structures (best resolution first).
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