Protein O-GlcNAcase (OGA) is a 916-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O60502.
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The mean pLDDT of this model is 74.8 (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 | 53% |
| 70 to 90 | Confident: backbone generally right | 15% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 27% |
What pLDDT means and how to read it
Cleaves GlcNAc but not GalNAc from O-glycosylated proteins (PubMed:11148210, PubMed:11788610, PubMed:20673219, PubMed:22365600, PubMed:24088714, PubMed:28939839, PubMed:37962578). Deglycosylates a large and diverse number of proteins, such as CRYAB, ELK1, GSDMD, LMNB1 and TAB1 (PubMed:28939839, PubMed:37962578). Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro) (PubMed:20673219). Does not bind acetyl-CoA and does not have histone acetyltransferase activity (PubMed:24088714)
Monomer (PubMed:11788610). Interacts with CLOCK (By similarity)
Nucleus, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5UN8 | X-ray | 2.13 Å | A/B/C/D=60-400, A/B/C/D=553-704 |
| 5M7U | X-ray | 2.3 Å | A/B=1-916 |
| 5M7R | X-ray | 2.35 Å | A/B=1-916 |
| 5M7S | X-ray | 2.4 Å | A/B=1-916 |
| 7OU6 | X-ray | 2.41 Å | AAA/BBB=1-916 |
| 5TKE | X-ray | 2.48 Å | A/B=60-400, A/B=553-704 |
| 5UN9 | X-ray | 2.5 Å | A/B=60-400, A/B=553-704 |
| 8P0L | X-ray | 2.5 Å | A/B=1-916 |
| 9BA8 | X-ray | 2.54 Å | A/B=55-713 |
| 2YDQ | X-ray | 2.6 Å | T=402-408 |
| 5M7T | X-ray | 2.6 Å | A/B=1-916 |
| 5VVO | X-ray | 2.6 Å | A/B=60-400, A/B=553-704 |
| 5VVU | X-ray | 2.7 Å | A/C=60-400, A/C=553-704 |
| 9BA9 | X-ray | 2.75 Å | A=55-713 |
| 5UHP | X-ray | 2.79 Å | A/B/C/D=14-400, E/F/G/H=554-705 |
| 5VVT | X-ray | 2.8 Å | A/C=60-400, A/C=553-704 |
| 5VVV | X-ray | 2.8 Å | A/C=60-400, A/C=553-704 |
| 6PM9 | X-ray | 2.86 Å | A/B/C/D=14-400, E/F/G/H=554-705 |
| 5VVX | X-ray | 2.9 Å | A/C=60-400, A/C=553-704 |
| 5UHK | X-ray | 2.97 Å | A/C=56-400, B/D=544-705 |
Showing 20 of 28 experimental structures (best resolution first).
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