1LYK
THE IMPACT OF THE PHYSICAL AND CHEMICAL ENVIROMENT ON THE MOLECULAR STRUCTURE OF COPRINUS CINEREUS PEROXIDASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000302 | biological_process | response to reactive oxygen species |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0034599 | biological_process | cellular response to oxidative stress |
| A | 0042744 | biological_process | hydrogen peroxide catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| A | 0140825 | molecular_function | lactoperoxidase activity |
| B | 0000302 | biological_process | response to reactive oxygen species |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0034599 | biological_process | cellular response to oxidative stress |
| B | 0042744 | biological_process | hydrogen peroxide catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0140825 | molecular_function | lactoperoxidase activity |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"PubMed","id":"8112469","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"O-linked (Man...) serine","evidences":[{"source":"PubMed","id":"8112469","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1apx |
| Chain | Residue | Details |
| A | ARG51 | |
| A | ASN92 | |
| A | HIS55 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1apx |
| Chain | Residue | Details |
| B | ARG51 | |
| B | ASN92 | |
| B | HIS55 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1apx |
| Chain | Residue | Details |
| A | ARG51 | |
| A | ASN84 | |
| A | HIS55 |
