1LY8
The crystal structure of a mutant enzyme of Coprinus cinereus peroxidase provides an understanding of its increased thermostability and insight into modelling of protein structures
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 | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | HIS55 | |
| B | HIS55 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP56 | |
| B | ASP56 | |
| B | GLY74 | |
| B | ASP76 | |
| B | SER78 | |
| B | SER184 | |
| B | ASP201 | |
| B | THR203 | |
| B | VAL206 | |
| B | ASP208 | |
| A | GLY74 | |
| A | ASP76 | |
| A | SER78 | |
| A | SER184 | |
| A | ASP201 | |
| A | THR203 | |
| A | VAL206 | |
| A | ASP208 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | HIS183 | |
| B | HIS183 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| A | ARG51 | |
| B | ARG51 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:8477731 |
| Chain | Residue | Details |
| A | GLN1 | |
| B | GLN1 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:8112469 |
| Chain | Residue | Details |
| A | ASN142 | |
| B | ASN142 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | CARBOHYD: O-linked (Man...) serine => ECO:0000269|PubMed:8112469 |
| Chain | Residue | Details |
| A | SER338 | |
| B | SER338 |
