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 | ACT_SITE: |
Chain | Residue | Details |
A | GLU183 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | CYS29 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
A | GLU104 | |
A | HIS105 | |
A | SER108 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:8747463 |
Chain | Residue | Details |
A | PCA0 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine |
Chain | Residue | Details |
A | ASN12 | |
A | ASN93 | |
A | ASN216 |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | CARBOHYD: O-linked (Man) threonine |
Chain | Residue | Details |
A | THR238 | |
A | THR250 | |
A | THR252 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | CARBOHYD: O-linked (Man) serine |
Chain | Residue | Details |
A | SER239 | |
A | SER241 | |
A | SER242 | |
A | SER251 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | CARBOHYD: O-linked (Man) serine => ECO:0000305 |
Chain | Residue | Details |
A | SER248 |
site_id | SWS_FT_FI9 |
Number of Residues | 3 |
Details | CARBOHYD: O-linked (Man...) threonine |
Chain | Residue | Details |
A | THR275 | |
A | THR283 | |
A | THR293 |
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 | CYS29 | activator, covalently attached, metal ligand |
A | HIS105 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | ASP106 | electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity |
A | GLU183 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |