2CJ2
chloroperoxidase complexed with formate (sugar cryoprotectant)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"O-linked (Man) threonine"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"O-linked (Man) serine"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"O-linked (Man) serine","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"O-linked (Man...) threonine"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2cpo |
| Chain | Residue | Details |
| A | GLU183 | |
| A | HIS105 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 250 |
| Chain | Residue | Details |
| A | ASN33 | activator, covalently attached, metal ligand |
| A | PHE109 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | SER110 | electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity |
| A | ILE187 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
