mRNA-capping enzyme (RNGTT) is a 597-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O60942.
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The mean pLDDT of this model is 85.4 (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 | 27% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 9% |
What pLDDT means and how to read it
Bifunctional mRNA-capping enzyme exhibiting RNA 5'-triphosphate monophosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the GMP moiety of GTP to the 5'-diphosphate terminus of RNA via a covalent enzyme-GMP reaction intermediate
Interacts with POLR2A (via C-terminus); this enhances guanylyltransferase activity. Binds (via GTase domain) to the elongating phosphorylated form of RNA polymerase II; can form direct interactions with the phosphorylated POLR2A C-terminal domain and indirect interactions via bound RNA (By similarity). Interacts with SUPT5H and RNMT. Interacts with HIV-1 Tat
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2C46 | X-ray | 1.6 Å | A/B/C/D=1-219 |
| 3S24 | X-ray | 3.01 Å | A/B/C/D/E/F/G=229-567 |
| 8P4B | EM | 3.2 Å | M=1-597 |
| 8P4A | EM | 3.6 Å | M=1-597 |
| 8P4D | EM | 3.6 Å | M=1-597 |
| 8P4C | EM | 3.8 Å | M=1-597 |
| 8P4E | EM | 3.9 Å | M=1-597 |
| 8W8E | EM | 3.9 Å | a=1-597 |
| 8W8F | EM | 4.0 Å | a=1-597 |
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