CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.379 | Chitobiase; domain 2 |
|
3.30.379.10 | Chitobiase/beta-hexosaminidase domain 2-like |
Domain Context
CATH Clusters
| Superfamily | Chitobiase/beta-hexosaminidase domain 2-like |
| Functional Family | O-GlcNAcase BT_4395 |
Enzyme Information
| 3.2.1.169 |
Protein O-GlcNAcase.
based on mapping to UniProt Q89ZI2
(1) [Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine + H(2)O = [protein]-L-serine + N-acetyl-D-glucosamine. (2) [Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine + H(2)O = [protein]-L-threonine + N-acetyl-D-glucosamine.
-!- Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. -!- EC 2.4.1.155 transfers GlcNAc onto substrate proteins and EC 3.2.1.169 cleaves GlcNAc from the modified proteins.
|
UniProtKB Entries (1)
| Q89ZI2 |
OGA_BACTN
Bacteroides thetaiotaomicron VPI-5482
O-GlcNAcase BT_4395
|
PDB Structure
| PDB | 2W67 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Molecular Basis for Inhibition of Gh84 Glycoside Hydrolases by Substituted Azepanes: Conformational Flexibility Enables Probing of Substrate Distortion.
J.Am.Chem.Soc.
|