Small ubiquitin-related modifier 1 (SUMO1) is a 101-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P63165.
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The mean pLDDT of this model is 78.3 (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 | 38% |
| 70 to 90 | Confident: backbone generally right | 36% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 17% |
What pLDDT means and how to read it
Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this…
Covalently attached to KCNB1; UBE2I increases cross-linking with KCNB1 and PIAS1 decreases cross-links with KCNB1 (PubMed:15931224, PubMed:19223394). Interacts with SAE2, RANBP2, PIAS1 and PIAS2 (PubMed:10961991, PubMed:15608651, PubMed:15660128, PubMed:15931224, PubMed:16204249). Interacts with PRKN (PubMed:16955485). Covalently attached to a number of proteins such as IKFZ1, PML, RANGAP1,…
Nucleus membrane, Nucleus speckle, Cytoplasm, Nucleus, PML body, Cell membrane, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6UYR | X-ray | 1.3 Å | A=17-97 |
| 4WJQ | X-ray | 1.35 Å | A/C=17-97 |
| 6V7Q | X-ray | 1.35 Å | A/C=17-97 |
| 2UYZ | X-ray | 1.4 Å | B=20-97 |
| 6UYV | X-ray | 1.4 Å | A=17-97 |
| 6UYZ | X-ray | 1.4 Å | A/C=17-97 |
| 6V7P | X-ray | 1.4 Å | A/C=17-97 |
| 6UYP | X-ray | 1.42 Å | A=17-97 |
| 4WJO | X-ray | 1.46 Å | A=17-97 |
| 6V7S | X-ray | 1.47 Å | A/C=17-97 |
| 4WJN | X-ray | 1.5 Å | A=17-97 |
| 6UYQ | X-ray | 1.5 Å | A=17-97 |
| 6V7R | X-ray | 1.55 Å | A/C=17-97 |
| 6UYS | X-ray | 1.59 Å | A/C=17-97 |
| 6UYY | X-ray | 1.6 Å | A=17-97 |
| 6UYO | X-ray | 1.64 Å | A/C=17-97 |
| 6UYT | X-ray | 1.66 Å | A=17-97 |
| 6UYU | X-ray | 1.66 Å | A/C=17-97 |
| 4WJP | X-ray | 1.7 Å | A/C=17-97 |
| 6UYX | X-ray | 1.7 Å | A/C=17-97 |
Showing 20 of 66 experimental structures (best resolution first).
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