UniProt O60502
Protein O-GlcNAcase (O60502)
Protein O-GlcNAcase (UniProt O60502), EC 3.2.1.-, 3.2.1.169: 38 experimental structures and 1 predicted model on GenesisL1, 9 ligands bound, 116 pockets. Binding sites, druggability and experiment against prediction (TM-score) in…
- UniProt
- O60502
- Protein
- Protein O-GlcNAcase
- EC
- 3.2.1.-, 3.2.1.169
- Experimental structures
- 38
- Predicted models
- 1
- Ligands
- 9
- Pockets
- 116 · 14 records with a druggable one
Structures
39 records of O60502 in the MolNFT archive: 38 experimental, 1 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 2YDQ | CpOGA D298N in complex with hOGA-derived O-GlcNAc peptide | x-ray diffraction | T | — | — |
| 2YDQ | Cpoga D298N in complex with hoga-derived O-glcnac peptide | x-ray diffraction | T | — | — |
| 5M7R | Structure of human O-GlcNAc hydrolase | x-ray diffraction | A, B | — | — |
| 5M7R | Structure of human O-glcnac hydrolase | x-ray diffraction | A, B | — | — |
| 5M7S | Structure of human O-GlcNAc hydrolase with bound transition state analog ThiametG | x-ray diffraction | A, B | NHT | 7 (best 0.82) |
| 5M7S | Structure of human O-glcnac hydrolase with bound transition state analog thiametg | x-ray diffraction | A, B | NHT | — |
| 5M7T | Structure of human O-GlcNAc hydrolase with PugNAc type inhibitor | x-ray diffraction | A, B | GDV | 7 (best 0.83) |
| 5M7T | Structure of human O-glcnac hydrolase with pugnac type inhibitor | x-ray diffraction | A, B | GDV | — |
| 5M7U | Structure of human O-GlcNAc hydrolase with new iminocyclitol type inhibitor | x-ray diffraction | A, B | XHA | 6 (best 0.79) |
| 5M7U | Structure of human O-glcnac hydrolase with new iminocyclitol type inhibitor | x-ray diffraction | A, B | XHA | — |
| 5TKE | Crystal structure of eukaryotic hydrolase | x-ray diffraction | A, B | — | — |
| 5UHK | Crystal structure of the core catalytic domain of Human O-GlcNAcase | x-ray diffraction | A, B, C, D | — | 6 (best 0.81) |
| 5UHK | Crystal structure of the core catalytic domain of human O-glcnacase | x-ray diffraction | A, B, C, D | — | — |
| 5UHL | Crystal structure of the core catalytic domain of human O-GlcNAcase complexed with Thiamet G | x-ray diffraction | A, B, C, D | 8BJ | 8 (best 0.79) |
| 5UHL | Crystal structure of the core catalytic domain of human O-glcnacase complexed with thiamet G | x-ray diffraction | A, B, C, D | 8BJ | — |
| 5UHO | Crystal structure of the core catalytic domain of human O-GlcNAcase complexed with PUGNAc | x-ray diffraction | A, B, C, D | OAN | — |
| 5UHO | Crystal structure of the core catalytic domain of human O-glcnacase complexed with pugnac | x-ray diffraction | A, B, C, D | OAN | — |
| 5UHP | Crystal structure of the core catalytic domain of human O-GlcNAcase | x-ray diffraction | A, B, C, D, E, F, G, H | — | — |
| 5UHP | Crystal structure of the core catalytic domain of human O-glcnacase | x-ray diffraction | A, B, C, D, E, F, G, H | — | — |
| 5UN8 | Crystal Structure of human O-GlcNAcase in complex with glycopeptide p53 | x-ray diffraction | A, B, C, D | NAG | 16 (best 0.82) |
| 5UN8 | Crystal structure of human O-glcnacase in complex with glycopeptide P53 | x-ray diffraction | A, B, C, D | NAG | — |
| 5UN9 | The crystal structure of human O-GlcNAcase in complex with Thiamet-G | x-ray diffraction | A, B | NHT | 5 (best 0.81) |
| 5UN9 | The crystal structure of human O-glcnacase in complex with thiamet-G | x-ray diffraction | A, B | NHT | — |
| 5VVO | Structural Investigations of the Substrate Specificity of Human O-GlcNAcase | x-ray diffraction | A, B | — | 6 (best 0.81) |
| 5VVO | Structural investigations of the substrate specificity of human O- glcnacase | x-ray diffraction | A, B | — | — |
| 5VVT | Structural Investigations of the Substrate Specificity of Human O-GlcNAcase | x-ray diffraction | A, C | NAG | 9 (best 0.81) |
| 5VVT | Structural investigations of the substrate specificity of human O- glcnacase | x-ray diffraction | A, C | NAG | — |
| 5VVU | Structural Investigations of the Substrate Specificity of Human O-GlcNAcase | x-ray diffraction | A, C | NAG | 6 (best 0.81) |
| 5VVU | Structural investigations of the substrate specificity of human O- glcnacase | x-ray diffraction | A, C | NAG | — |
| 5VVV | Structural Investigations of the Substrate Specificity of Human O-GlcNAcase | x-ray diffraction | A, C | NAG | — |
| 5VVV | Structural investigations of the substrate specificity of human O- glcnacase | x-ray diffraction | A, C | NAG | — |
| 5VVX | Structural investigations of the substrate specificity of human O- glcnacase | x-ray diffraction | A, C | NAG | — |
| 6HKI | Crystal structure of surface entropy mutant of human O-GlcNAc hydrolase | x-ray diffraction | A, B | — | 8 (best 0.83) |
| 6HKI | Crystal structure of surface entropy mutant of human O-glcnac hydrolase | x-ray diffraction | A, B | — | — |
| 6PM9 | Crystal structure of the core catalytic domain of human O-GlcNAcase bound to MK-8719 | x-ray diffraction | A, B, C, D, E, F, G, H | OQ1 | 20 (best 0.77) |
| 6PM9 | Crystal structure of the core catalytic domain of human O-glcnacase bound to mk-8719 | x-ray diffraction | A, B, C, D, E, F, G, H | OQ1 | — |
| 7OU6 | Human O-GlcNAc hydrolase in complex with DNJNAc-thiazolidines | x-ray diffraction | AAA, BBB | 1XI | 5 (best 0.80) |
| 7YEH | Cryo-EM structure of human OGT-OGA complex | electron microscopy | C, D | UDP, NAG | — |
| O60502 | AlphaFold monomer V2.0 prediction for protein O-glcnacase (O60502) | predicted | A | — | 7 (best 0.78) |
Ligands
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · in 10 records
- NHT · (3ar,5r,6s,7r,7ar)-2-(ethylamino)-5-(hydroxymethyl)-5, 6,7,7A-tetrahydro-3AH-pyrano[3,2-d][1,3]thiazole-6,7-diol · in 4 records
- 8BJ · (2z,3ar,5r,6s,7r,7ar)-2-(ethylimino)-5-(hydroxymethyl) hexahydro-3AH-pyrano[3,2-d][1,3]thiazole-6,7-diol · in 2 records
- GDV · (5R,6R,7R,8S)-8-(acetylamino)-6,7-dihydroxy-5-(hydroxymethyl)-N-phenyl-1,5,6,7,8,8A-hexahydroimidazo[1,2-a]pyridine-2-carboxamide · in 2 records
- OAN · O-(2-acetamido-2-deoxy D-glucopyranosylidene) amino-N-phenylcarbamate · in 2 records
- OQ1 · (3ar,5s,6s,7r,7ar)-5-(difluoromethyl)-2-(ethylamino)-5, 6,7,7A-tetrahydro-3AH-pyrano[3,2-d][1,3]thiazole-6,7-diol · in 2 records
- XHA · 2-[(2~{R},3~{S},4~{R},5~{R})-5-(hydroxymethyl)-3,4-bis(oxidanyl)-1-[3-[3-(trifluoromethyl) phenyl]propyl]pyrrolidin-2-yl]-~{N}-methyl-ethanamide · in 2 records
- 1XI · ~{N}-[(3~{Z},6~{S},7~{R},8~{R},8~{a}~{S})-7,8-bis(oxidanyl)-3-(phenylmethyl)imino-1,5,6,7,8,8~{a}-hexahydro-[1,3]thiazolo[3,4-a]pyridin-6-yl]ethanamide · in 1 record
- UDP · Uridine-5'-diphosphate · in 1 record
Experiment against prediction
- 5UHO chain C against the predicted model O60502: TM-score 0.99, RMSD 0.52 Å
- 5UHO chain C against the predicted model O60502: TM-score 0.99, RMSD 0.52 Å
- 5UHL chain C against the predicted model O60502: TM-score 0.99, RMSD 0.52 Å
- 5UHL chain C against the predicted model O60502: TM-score 0.99, RMSD 0.52 Å
- 5UHK chain C against the predicted model O60502: TM-score 0.99, RMSD 0.59 Å
- 5UHK chain C against the predicted model O60502: TM-score 0.99, RMSD 0.59 Å
- 5UHL chain A against the predicted model O60502: TM-score 0.99, RMSD 0.60 Å
- 5UHL chain A against the predicted model O60502: TM-score 0.99, RMSD 0.60 Å
- 5UHO chain A against the predicted model O60502: TM-score 0.99, RMSD 0.62 Å
- 5UHO chain A against the predicted model O60502: TM-score 0.99, RMSD 0.62 Å
Elsewhere
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