Small ubiquitin-related modifier 2 (SUMO2) is a 95-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P61956.
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The mean pLDDT of this model is 83.8 (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 | 61% |
| 70 to 90 | Confident: backbone generally right | 17% |
| 50 to 70 | Low: treat with caution | 17% |
| Below 50 | Very low: often disordered regions | 5% |
What pLDDT means and how to read it
Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as 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 an E3 ligase such as PIAS1-4, RANBP2, CBX4 or ZNF451 (PubMed:26524494). 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. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of…
Interacts with SAE2 and UBE2I. Interacts with ZNF451. Identified in a complex with ZNF451 and UBE2I/UBC9, where one ZNF451 interacts with one UBE2I/UBC9 and two SUMO2 chains, one bound to the UBE2I/UBC9 active site and the other to another region of the same UBE2I/UBC9 molecule. Covalently attached to a number of proteins. Interacts with PELP1. Interacts with USP25; the interaction sumoylates…
Nucleus, Nucleus, PML body
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1WM3 | X-ray | 1.2 Å | A=17-88 |
| 1WM2 | X-ray | 1.6 Å | A=12-89 |
| 4NPN | X-ray | 1.63 Å | A=12-93 |
| 2D07 | X-ray | 2.1 Å | B=1-93 |
| 4BKG | X-ray | 2.11 Å | A=9-93 |
| 3ZO5 | X-ray | 2.15 Å | B=16-95 |
| 2IO0 | X-ray | 2.3 Å | B=15-95 |
| 5ELU | X-ray | 2.35 Å | B=14-89 |
| 5D2M | X-ray | 2.4 Å | B/E=15-93 |
| 7ZJV | X-ray | 2.4 Å | B=18-92 |
| 5EQL | X-ray | 2.49 Å | B=14-89 |
| 3UIN | X-ray | 2.6 Å | B=14-93 |
| 3UIO | X-ray | 2.6 Å | B=14-93 |
| 2CKH | X-ray | 3.2 Å | B=15-93 |
| 2IO3 | X-ray | 3.2 Å | B=15-93 |
| 2IYD | X-ray | 3.2 Å | B=15-95 |
| 1WZ0 | NMR | A=1-91 | |
| 2AWT | NMR | A=1-95 | |
| 2N1W | NMR | A=1-93 | |
| 2N9E | NMR | B=1-95 |
Showing 20 of 25 experimental structures (best resolution first).
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