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 | 15 |
Details | BINDING SITE FOR RESIDUE CIT A 201 |
Chain | Residue |
A | ASN118 |
A | HOH207 |
A | HOH326 |
A | HOH360 |
A | HOH370 |
A | HOH394 |
A | HOH405 |
A | GLU124 |
A | HIS134 |
A | SER136 |
A | ALA142 |
A | GLY143 |
A | ILE155 |
A | PRO161 |
A | HOH203 |
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 | 2 |
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 | |