SUMO-conjugating enzyme UBC9 (UBE2I) is a 158-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P63279.
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The mean pLDDT of this model is 97.3 (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 | 98% |
| 70 to 90 | Confident: backbone generally right | 1% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3, SUMO4 and SUMO1P1/SUMO5 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2, CBX4 and ZNF451. Can catalyze the formation of poly-SUMO chains. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation. Sumoylates p53/TP53 at 'Lys-386'. Mediates sumoylation of ERCC6 which is essential for its transcription-coupled nucleotide excision repair activity (PubMed:26620705). Sumoylates SHMT1 at 'Lys-38' or 'Lys-39' leading to RAN-dependent nuclear import of SHMT1 (PubMed:17446168). Also sumoylates TYMS and DHFR…
Forms a complex with SENP6 and UBE2I in response to UV irradiation (PubMed:17704809). Forms a tight complex with RANGAP1 and RANBP2 (PubMed:11853669, PubMed:15378033, PubMed:15608651, PubMed:15931224, PubMed:16732283). Identified in a complex with SUMO2 and UBE2I, where one ZNF451 interacts with one UBE2I and two SUMO2 chains, one bound to the UBE2I active site and the other to another region of…
Nucleus, Cytoplasm, Cytoplasm, perinuclear region
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5F6E | X-ray | 1.12 Å | A=2-158 |
| 5F6Y | X-ray | 1.14 Å | A=2-158 |
| 2GRR | X-ray | 1.3 Å | A=1-158 |
| 5F6V | X-ray | 1.49 Å | A=2-158 |
| 5F6D | X-ray | 1.55 Å | A=2-158 |
| 5F6U | X-ray | 1.55 Å | A=2-158 |
| 5F6X | X-ray | 1.56 Å | A=2-158 |
| 2GRO | X-ray | 1.7 Å | A=1-158 |
| 2GRQ | X-ray | 1.7 Å | A=1-158 |
| 5F6W | X-ray | 1.7 Å | A=2-158 |
| 9GLR | X-ray | 1.72 Å | AAA=1-158 |
| 2GRN | X-ray | 1.8 Å | A=1-158 |
| 6SYF | X-ray | 1.9 Å | A/B/C/D=2-158 |
| 2GRP | X-ray | 2.05 Å | A=1-158 |
| 5FQ2 | X-ray | 2.2 Å | A=1-158 |
| 3UIP | X-ray | 2.29 Å | A=1-158 |
| 2PE6 | X-ray | 2.4 Å | A=1-158 |
| 5D2M | X-ray | 2.4 Å | A/D=1-158 |
| 1KPS | X-ray | 2.5 Å | A/C=1-158 |
| 4W5V | X-ray | 2.5 Å | A=1-158 |
Showing 20 of 33 experimental structures (best resolution first).
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