1LY9
The impact of the physical and chemical environment 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 | 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 | 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 PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 9001 |
Chain | Residue |
B | SER184 |
B | ASP201 |
B | THR203 |
B | VAL206 |
B | ASP208 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 9002 |
Chain | Residue |
A | ASP208 |
A | SER184 |
A | ASP201 |
A | THR203 |
A | VAL206 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 9003 |
Chain | Residue |
A | ASP56 |
A | GLY74 |
A | ASP76 |
A | SER78 |
A | HOH1009 |
A | HOH1027 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 9004 |
Chain | Residue |
B | ASP56 |
B | GLY74 |
B | ASP76 |
B | SER78 |
B | HOH2009 |
B | HOH2027 |
site_id | AC5 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE HEM A 344 |
Chain | Residue |
A | ARG47 |
A | LEU50 |
A | ARG51 |
A | PHE54 |
A | GLY154 |
A | PRO155 |
A | LEU180 |
A | ALA182 |
A | HIS183 |
A | LEU185 |
A | ALA186 |
A | SER187 |
A | GLU189 |
A | GLY190 |
A | LEU191 |
A | MET242 |
A | SER244 |
A | MET276 |
A | HOH1010 |
A | HOH1011 |
A | HOH1014 |
A | HOH3054 |
site_id | AC6 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEM B 344 |
Chain | Residue |
A | HOH3091 |
B | ARG47 |
B | LEU50 |
B | ARG51 |
B | PHE54 |
B | GLY154 |
B | PRO155 |
B | LEU179 |
B | LEU180 |
B | ALA182 |
B | HIS183 |
B | LEU185 |
B | ALA186 |
B | SER187 |
B | GLU189 |
B | GLY190 |
B | LEU191 |
B | MET242 |
B | SER244 |
B | MET276 |
B | HOH2010 |
B | HOH2011 |
B | HOH2014 |
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 | SER142 | |
B | SER142 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | CARBOHYD: O-linked (Man...) serine => ECO:0000269|PubMed:8112469 |
Chain | Residue | Details |
A | ALA338 | |
B | ALA338 |