Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006486 | biological_process | protein glycosylation |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| A | 0018279 | biological_process | protein N-linked glycosylation via asparagine |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE FLC A 1 |
| Chain | Residue |
| A | ASN118 |
| A | HOH217 |
| A | HOH298 |
| A | HOH311 |
| A | GLU124 |
| A | HIS134 |
| A | SER136 |
| A | VAL137 |
| A | GLY143 |
| A | PHE152 |
| A | ILE155 |
| A | PRO161 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"18667421","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18667421","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Increases basicity of active site His"} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1lxa |
| Chain | Residue | Details |
| A | HIS125 | |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1lxa |
| Chain | Residue | Details |
| A | PRO161 | |
