1OMX
Crystal structure of mouse alpha-1,4-N-acetylhexosaminyltransferase (EXTL2)
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 401 |
| Chain | Residue |
| A | PHE171 |
| A | GLN174 |
| A | PRO260 |
| A | ILE314 |
| A | HOH432 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 402 |
| Chain | Residue |
| B | HOH417 |
| B | PHE171 |
| B | GLN174 |
| B | PRO260 |
| B | ILE263 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 403 |
| Chain | Residue |
| A | LYS222 |
| A | TYR223 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"12562774","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12562774","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ON6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ON8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12562774","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ON6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
