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2J5M

Structure of Chloroperoxidase Compound 0

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsGlycosylation: {"description":"O-linked (Man) threonine"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsGlycosylation: {"description":"O-linked (Man) serine"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (Man) serine","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsGlycosylation: {"description":"O-linked (Man...) threonine"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2cpo
ChainResidueDetails
AGLU183
AHIS105

site_idMCSA1
Number of Residues4
DetailsM-CSA 250
ChainResidueDetails
AASN33activator, covalently attached, metal ligand
APHE109electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ASER110electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity
AILE187activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay

238895

PDB entries from 2025-07-16

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