S-phase kinase-associated protein 2 (SKP2) is a 424-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13309.
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The mean pLDDT of this model is 82.1 (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 | 72% |
| 70 to 90 | Confident: backbone generally right | 4% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 19% |
What pLDDT means and how to read it
Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription (PubMed:9736735, PubMed:11931757, PubMed:12435635, PubMed:12769844, PubMed:12840033, PubMed:15342634, PubMed:15668399, PubMed:15949444, PubMed:16103164, PubMed:16262255, PubMed:16581786, PubMed:16951159, PubMed:17908926, PubMed:17962192, PubMed:22464731, PubMed:22770219, PubMed:32267835). Specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition (By similarity). Degradation of…
Part of a SCF(SKP2) complex consisting of CUL1, RBX1, SKP1 and SKP2. Component of a SCF(SKP2)-like complex containing CUL1, SKP1, TRIM21 and SKP2. Interacts directly with CUL1 and SKP1. Interacts with CKS1. Interacts with ASB2 which is the substrate-recognition component of a probable ECS E3 ubiquitin-protein ligase complex; ASB2 is likely to bridge the formation of dimeric E3-ubiquitin-protein…
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1FS1 | X-ray | 1.8 Å | A/C=89-141 |
| 2AST | X-ray | 2.3 Å | B=89-424 |
| 7Z8V | EM | 2.7 Å | F=1-424 |
| 1FQV | X-ray | 2.8 Å | A/C/E/G/I/K/M/O=89-424 |
| 1FS2 | X-ray | 2.9 Å | A/C=89-398 |
| 8OR3 | EM | 2.9 Å | E=1-424 |
| 9QO4 | EM | 2.95 Å | M=1-424 |
| 2ASS | X-ray | 3.0 Å | B=89-424 |
| 7Z8T | EM | 3.0 Å | F=1-424 |
| 1LDK | X-ray | 3.1 Å | E=97-137 |
| 7ZBZ | EM | 3.1 Å | F=1-424 |
| 8OR0 | EM | 3.1 Å | E=1-424 |
| 7LUO | X-ray | 3.17 Å | A/C=17-83 |
| 9QO0 | EM | 3.26 Å | M=1-424 |
| 8CDK | EM | 3.32 Å | F=1-424 |
| 8BYA | EM | 3.38 Å | E=1-424 |
| 8CDJ | EM | 3.4 Å | F=1-424 |
| 7ZBW | EM | 3.5 Å | F=1-424 |
| 8BYL | EM | 3.5 Å | B=1-424 |
| 7B5L | EM | 3.8 Å | T=1-424 |
Showing 20 of 26 experimental structures (best resolution first).
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