3SI2
Structure of glycosylated murine glutaminyl cyclase in presence of the inhibitor PQ50 (PDBD150)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016603 | molecular_function | glutaminyl-peptide cyclotransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0017186 | biological_process | peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q16769","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21671571","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3SI1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SI2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"21671571","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3SI1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SI2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
