2CPO
CHLOROPEROXIDASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
Functional Information from PDB Data
| site_id | HE1 |
| Number of Residues | 2 |
| Details | HEME PROXIMAL SITE. |
| Chain | Residue |
| A | HEM396 |
| A | CYS29 |
| site_id | HEM |
| Number of Residues | 5 |
| Details | HEME DISTAL SITE. |
| Chain | Residue |
| A | HEM396 |
| A | GLU183 |
| A | HIS105 |
| A | PHE186 |
| A | HOH801 |
| site_id | MN |
| Number of Residues | 7 |
| Details | MANGANESE BINDING SITE. |
| Chain | Residue |
| A | GLU104 |
| A | HIS105 |
| A | SER108 |
| A | HOH802 |
| A | HOH803 |
| A | MN301 |
| A | HEM396 |
| site_id | NG1 |
| Number of Residues | 2 |
| Details | N-GLYCOSYLATION SITE. |
| Chain | Residue |
| A | ASN12 |
| A | NAG512 |
| site_id | NG2 |
| Number of Residues | 3 |
| Details | N-GLYCOSYLATION SITE. |
| Chain | Residue |
| A | ASN93 |
| B | NAG1 |
| B | NAG2 |
| site_id | NG3 |
| Number of Residues | 3 |
| Details | N-GLYCOSYLATION SITE. |
| Chain | Residue |
| A | ASN216 |
| C | NAG1 |
| C | NAG2 |
| site_id | OG1 |
| Number of Residues | 2 |
| Details | O-GLYCOSYLATION SITE. |
| Chain | Residue |
| A | THR238 |
| A | MAN738 |
| site_id | OG2 |
| Number of Residues | 2 |
| Details | O-GLYCOSYLATION SITE. |
| Chain | Residue |
| A | SER239 |
| A | MAN739 |
| site_id | OG3 |
| Number of Residues | 2 |
| Details | O-GLYCOSYLATION SITE. |
| Chain | Residue |
| A | SER241 |
| A | MAN741 |
| site_id | OG4 |
| Number of Residues | 2 |
| Details | O-GLYCOSYLATION SITE. |
| Chain | Residue |
| A | SER242 |
| A | MAN742 |
| site_id | OG5 |
| Number of Residues | 2 |
| Details | O-GLYCOSYLATION SITE. |
| Chain | Residue |
| A | SER248 |
| A | MAN748 |
| site_id | OG6 |
| Number of Residues | 2 |
| Details | O-GLYCOSYLATION SITE. |
| Chain | Residue |
| A | THR250 |
| A | MAN750 |
| site_id | OG7 |
| Number of Residues | 2 |
| Details | O-GLYCOSYLATION SITE. |
| Chain | Residue |
| A | SER251 |
| A | MAN751 |
| site_id | OG8 |
| Number of Residues | 2 |
| Details | O-GLYCOSYLATION SITE. |
| Chain | Residue |
| A | THR252 |
| A | MAN752 |
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 | a catalytic site defined by CSA, PubMed 9751642 |
| 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 |
