NEDD8-activating enzyme E1 regulatory subunit (NAE1) is a 534-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13564.
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The mean pLDDT of this model is 96.3 (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 | 94% |
| 70 to 90 | Confident: backbone generally right | 6% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Regulatory subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Necessary for cell cycle progression through the S-M checkpoint. Overexpression of NAE1 causes apoptosis through deregulation of NEDD8 conjugation. The covalent attachment of NEDD8 to target proteins is known as 'neddylation' and the process is involved in the regulation of cell growth, viability and development
Heterodimer of UBA3 and NAE1. The complex binds NEDD8 and UBE2M. Binds APP and TP53BP2
Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1TT5 | X-ray | 2.6 Å | A/C=1-534 |
| 1YOV | X-ray | 2.6 Å | A/C=1-534 |
| 2NVU | X-ray | 2.8 Å | A=1-534 |
| 3DBH | X-ray | 2.85 Å | A/C/E/G=1-534 |
| 3DBL | X-ray | 2.9 Å | A/C/E/G=1-534 |
| 1R4M | X-ray | 3.0 Å | A/C/E/G=1-534 |
| 3GZN | X-ray | 3.0 Å | A/C=1-534 |
| 3DBR | X-ray | 3.05 Å | A/C/E/G=1-534 |
| 1R4N | X-ray | 3.6 Å | A/C/E/G=1-534 |
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