UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (OGT) is a 1046-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O15294.
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The mean pLDDT of this model is 93.1 (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 | 89% |
| 70 to 90 | Confident: backbone generally right | 6% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc) (PubMed:12150998, PubMed:15361863, PubMed:19451179, PubMed:20018868, PubMed:21240259, PubMed:21285374, PubMed:23103939, PubMed:26237509, PubMed:26369908, PubMed:26678539, PubMed:27713473, PubMed:37541260, PubMed:37962578). Glycosylates a large and diverse number of proteins including histone H2B, AKT1, AMPK, ATG4B, CAPRIN1, EZH2, FNIP1, GSDMD, KRT7, LMNA, LMNB1, LMNB2, RPTOR, HOXA1, PFKL, KMT2E/MLL5, MAPT/TAU, TET2, RBL2, RET, NOD2 and HCFC1 (PubMed:19451179,…
Monomer; may exist in different oligomerization states in cells (PubMed:21240259, PubMed:27713473). Homotrimer, oligomerizes via TPR repeats 6 and 7. Trimerization is not necessary for activity in vitro, however it increases affinity for UDP-GlcNAc (By similarity). Component of a THAP1/THAP3-HCFC1-OGT complex (PubMed:12670868, PubMed:20200153). Component of the NSL complex at least composed of…
Nucleus, Cytoplasm, Mitochondrion, Membrane, Cell membrane, Mitochondrion membrane, Cell projection
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5NPS | X-ray | 1.68 Å | A=324-1041 |
| 4GYW | X-ray | 1.7 Å | A/C=323-1041 |
| 6EOU | X-ray | 1.75 Å | A=26-410 |
| 4N39 | X-ray | 1.76 Å | A=323-1041 |
| 4GYY | X-ray | 1.85 Å | A/C=323-1041 |
| 5NPR | X-ray | 1.85 Å | A=325-1041 |
| 3TAX | X-ray | 1.88 Å | A/C=323-1041 |
| 4N3A | X-ray | 1.88 Å | A=323-1041 |
| 4GZ3 | X-ray | 1.9 Å | A/C=323-1041 |
| 5LWV | X-ray | 1.9 Å | A=325-1046 |
| 6TKA | X-ray | 1.91 Å | AAA=323-1046 |
| 3PE4 | X-ray | 1.95 Å | A/C=323-1041 |
| 6MA3 | X-ray | 2.0 Å | A=323-1041 |
| 6MA4 | X-ray | 2.0 Å | A=323-1041 |
| 6MA5 | X-ray | 2.0 Å | A=323-1041 |
| 5C1D | X-ray | 2.05 Å | A=323-1041 |
| 5HGV | X-ray | 2.05 Å | A/C=323-1041 |
| 6MA2 | X-ray | 2.1 Å | A=323-1041 |
| 4N3B | X-ray | 2.17 Å | A=323-1041 |
| 6IBO | X-ray | 2.17 Å | A=323-1041 |
Showing 20 of 44 experimental structures (best resolution first).
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