5GGF
Crystal structure of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase form II
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008375 | molecular_function | acetylglucosaminyltransferase activity |
| A | 0009101 | biological_process | glycoprotein biosynthetic process |
| B | 0008375 | molecular_function | acetylglucosaminyltransferase activity |
| B | 0009101 | biological_process | glycoprotein biosynthetic process |
| C | 0008375 | molecular_function | acetylglucosaminyltransferase activity |
| C | 0009101 | biological_process | glycoprotein biosynthetic process |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 483 |
| Details | Domain: {"description":"GG-type lectin","evidences":[{"source":"PROSITE-ProRule","id":"PRU01375","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 39 |
| Details | Region: {"description":"Interaction with O-glycosylated substrate glycoprotein","evidences":[{"source":"PubMed","id":"27493216","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27493216","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 21 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27493216","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5GGI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27493216","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5GGI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
