S-phase kinase-associated protein 1 (SKP1) is a 163-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P63208.
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The mean pLDDT of this model is 90.1 (very high 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 | 72% |
| 70 to 90 | Confident: backbone generally right | 18% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Essential component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as an adapter that links the F-box protein to CUL1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5, CEP68 and probably NFKB2 (PubMed:25704143). SCF(SKP2) directs…
Interacts with KDM2B, forming heterodimers (PubMed:27568929). The KDM2B-SKP1 heterodimeric complex interacts with the PCGF1-BCORL heterodimeric complex to form a homotetrameric polycomb repression complex 1 (PRC1.1) (PubMed:27568929). Component of multiple SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complexes formed of CUL1, SKP1, RBX1 and a variable F-box domain-containing protein as…
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1FS1 | X-ray | 1.8 Å | B/D=1-147 |
| 6M90 | X-ray | 2.05 Å | B=2-163 |
| 2AST | X-ray | 2.3 Å | A=2-160 |
| 6M92 | X-ray | 2.35 Å | B=2-163 |
| 2E31 | X-ray | 2.4 Å | B=1-163 |
| 6M91 | X-ray | 2.4 Å | B=2-163 |
| 2OVR | X-ray | 2.5 Å | A=1-69, A=82-163 |
| 5IBK | X-ray | 2.5 Å | A/D=1-69, A/D=82-163 |
| 6M93 | X-ray | 2.5 Å | B=2-163 |
| 6O60 | X-ray | 2.5 Å | D=1-163 |
| 6WNX | X-ray | 2.5 Å | B/E/H=1-163 |
| 5JH5 | X-ray | 2.55 Å | B=2-163 |
| 7T1Y | X-ray | 2.55 Å | A=1-163 |
| 2OVQ | X-ray | 2.6 Å | A=1-69, A=82-163 |
| 3WSO | X-ray | 2.6 Å | B=1-163 |
| 5V4B | X-ray | 2.6 Å | A=1-69, A=82-163 |
| 6BYH | X-ray | 2.61 Å | A/B/G=1-163 |
| 6BVA | X-ray | 2.66 Å | C/D=1-163 |
| 4I6J | X-ray | 2.7 Å | C=1-163 |
| 5VZT | X-ray | 2.7 Å | A/C=1-163 |
Showing 20 of 72 experimental structures (best resolution first).
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