5M7U
Structure of human O-GlcNAc hydrolase with new iminocyclitol type inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004415 | molecular_function | hyalurononglucosaminidase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006044 | biological_process | N-acetylglucosamine metabolic process |
| A | 0006493 | biological_process | protein O-linked glycosylation |
| A | 0006516 | biological_process | glycoprotein catabolic process |
| A | 0006517 | biological_process | protein deglycosylation |
| A | 0009100 | biological_process | glycoprotein metabolic process |
| A | 0015929 | molecular_function | hexosaminidase activity |
| A | 0016020 | cellular_component | membrane |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0102571 | molecular_function | [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity |
| B | 0004415 | molecular_function | hyalurononglucosaminidase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006044 | biological_process | N-acetylglucosamine metabolic process |
| B | 0006493 | biological_process | protein O-linked glycosylation |
| B | 0006516 | biological_process | glycoprotein catabolic process |
| B | 0006517 | biological_process | protein deglycosylation |
| B | 0009100 | biological_process | glycoprotein metabolic process |
| B | 0015929 | molecular_function | hexosaminidase activity |
| B | 0016020 | cellular_component | membrane |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0102571 | molecular_function | [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue XHA A 1001 |
| Chain | Residue |
| A | GLY67 |
| A | TRP278 |
| A | ASN280 |
| A | ASP285 |
| A | TYR286 |
| A | ASN313 |
| B | TRP645 |
| B | SER649 |
| B | TRP679 |
| A | PHE68 |
| A | TYR69 |
| A | LYS98 |
| A | ASP174 |
| A | ASP175 |
| A | TYR219 |
| A | THR250 |
| A | VAL254 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue XHA B 1001 |
| Chain | Residue |
| A | TRP645 |
| A | SER649 |
| A | TRP679 |
| B | GLY67 |
| B | PHE68 |
| B | LYS98 |
| B | ASP174 |
| B | ASP175 |
| B | TYR219 |
| B | THR250 |
| B | VAL254 |
| B | TRP278 |
| B | ASN280 |
| B | ASP285 |
| B | TYR286 |
| B | ASN313 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 552 |
| Details | Domain: {"description":"GH84","evidences":[{"source":"PROSITE-ProRule","id":"PRU01353","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01353","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16533067","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28939839","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5VVT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
