C-C chemokine receptor type 5 (CCR5) is a 352-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P51681.
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The mean pLDDT of this model is 85.4 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 65% |
| 70 to 90 | Confident: backbone generally right | 19% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 13% |
What pLDDT means and how to read it
Receptor for a number of inflammatory CC-chemokines including CCL3/MIP-1-alpha, CCL4/MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. May play a role in the control of granulocytic lineage proliferation or differentiation. Participates in T-lymphocyte migration to the infection site by acting as a chemotactic receptor (PubMed:30713770)
Interacts with PRAF2 (PubMed:15757671). Efficient ligand binding to CCL3/MIP-1alpha and CCL4/MIP-1beta requires sulfation, O-glycosylation and sialic acid modifications. Glycosylation on Ser-6 is required for efficient binding of CCL4 (PubMed:10383387, PubMed:11733580, PubMed:8663314, PubMed:8699119). Interacts with GRK2 (PubMed:10085131). Interacts with ARRB1 and ARRB2 (PubMed:11448957,…
Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5YD3 | X-ray | 1.35 Å | B/D/F/H=11-19 |
| 5YD4 | X-ray | 1.35 Å | B/D/F/H=11-19 |
| 5YY4 | X-ray | 1.59 Å | B=11-19 |
| 9J8A | X-ray | 1.75 Å | P=8-18 |
| 5YD5 | X-ray | 1.96 Å | B/D=11-19 |
| 5UIW | X-ray | 2.2 Å | A=2-352 |
| 7F1T | X-ray | 2.6 Å | A=2-223, A=227-319 |
| 4MBS | X-ray | 2.71 Å | A/B=2-352 |
| 6AKX | X-ray | 2.8 Å | A/B=2-223, A/B=227-319 |
| 6AKY | X-ray | 2.8 Å | A=2-223, A=227-319 |
| 7F1S | EM | 2.8 Å | R=2-319 |
| 7F1Q | EM | 2.9 Å | R=2-319 |
| 7F1R | EM | 3.0 Å | R=2-319 |
| 7O7F | EM | 3.15 Å | C=1-352 |
| 7NJZ | X-ray | 3.2 Å | C=8-13 |
| 7NW3 | X-ray | 3.2 Å | A=8-13 |
| 8AS2 | X-ray | 3.2 Å | B=331-352 |
| 8AS3 | X-ray | 3.5 Å | B=331-351 |
| 6MEO | EM | 3.9 Å | B=1-313 |
| 6MET | EM | 4.5 Å | B=1-313 |
Showing 20 of 25 experimental structures (best resolution first).
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