Stromal cell-derived factor 1 (CXCL12) is a 93-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P48061.
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The mean pLDDT of this model is 83.3 (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 | 32% |
| 70 to 90 | Confident: backbone generally right | 52% |
| 50 to 70 | Low: treat with caution | 16% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Chemoattractant active on T-lymphocytes and monocytes but not neutrophils (PubMed:18802065, PubMed:39093700). Activates the C-X-C chemokine receptor CXCR4 to induce a rapid and transient rise in the level of intracellular calcium ions and chemotaxis (PubMed:8752281, PubMed:18802065, PubMed:39093700). Also binds to atypical chemokine receptor ACKR3, which activates the beta-arrestin pathway and acts as a scavenger receptor for CXCL12/SDF-1 (PubMed:16107333, PubMed:19255243). Binds to the allosteric site (site 2) of integrins and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1 in a CXCR4-independent manner (PubMed:29301984). Acts as a positive regulator of monocyte migration and…
Monomer or homodimer; in equilibrium (PubMed:15741341). Dimer formation is induced by non acidic pH and the presence of multivalent anions, and by binding to CXCR4 or heparin (PubMed:15741341). Monomeric form is required for full chemotactic activity and resistance to ischemia/reperfusion injury, whereas the dimeric form acts as a partial agonist of CXCR4, stimulating Ca2+ mobilization but with…
Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3GV3 | X-ray | 1.6 Å | A=26-88 |
| 6SHR | X-ray | 1.75 Å | A=26-89 |
| 4UAI | X-ray | 1.9 Å | A/B=22-89 |
| 2J7Z | X-ray | 1.95 Å | A/B=22-89 |
| 1QG7 | X-ray | 2.0 Å | A/B=22-88 |
| 2NWG | X-ray | 2.07 Å | A/B=22-88 |
| 1A15 | X-ray | 2.2 Å | A/B=22-88 |
| 3HP3 | X-ray | 2.2 Å | A/B/C/D/E/F/G/H/I/J=22-88 |
| 9UPV | EM | 2.7 Å | J=22-29 |
| 4LMQ | X-ray | 2.77 Å | D/F=29-89 |
| 9UPU | EM | 2.8 Å | J=22-29 |
| 8K3Z | EM | 2.81 Å | D=22-83 |
| 8U4O | EM | 3.29 Å | J=22-89 |
| 7SK4 | EM | 3.3 Å | B=22-89 |
| 7SK7 | EM | 3.3 Å | B=22-89 |
| 7SK8 | EM | 3.3 Å | B=22-89 |
| 9ME1 | EM | 3.37 Å | F/G/H/J/M/N/O/P=22-93 |
| 9E82 | EM | 3.4 Å | B=25-89 |
| 9MEU | EM | 3.46 Å | F/G/H/J/M/N/O/P=22-93 |
| 7SK3 | EM | 3.8 Å | B=22-89 |
Showing 20 of 34 experimental structures (best resolution first).
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