Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004601 | molecular_function | peroxidase activity |
A | 0006979 | biological_process | response to oxidative stress |
A | 0020037 | molecular_function | heme binding |
A | 0034599 | biological_process | cellular response to oxidative stress |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEM A 295 |
Chain | Residue |
A | HIS175 |
A | LEU177 |
A | GLY178 |
A | LYS179 |
A | THR180 |
A | HIS181 |
A | ASN184 |
A | SER185 |
A | AMT296 |
A | HOH302 |
A | HOH311 |
A | HOH313 |
A | HOH314 |
A | PRO44 |
A | VAL47 |
A | TRP51 |
A | ASP146 |
A | LEU171 |
A | ALA174 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE AMT A 296 |
Chain | Residue |
A | HIS175 |
A | LEU177 |
A | THR180 |
A | LEU232 |
A | ASP235 |
A | HEM295 |
A | HOH401 |
site_id | AVE |
Number of Residues | 3 |
Details | REMOVAL OF TRP 191 FORMS AN INTERNAL CAVITY BELOW THE HEME RELATIVE TO THE ACTIVE SITE. |
Chain | Residue |
A | ARG48 |
A | TRP51 |
A | HIS52 |
Functional Information from PROSITE/UniProt
site_id | PS00435 |
Number of Residues | 11 |
Details | PEROXIDASE_1 Peroxidases proximal heme-ligand signature. EVVALMGAHAL |
Chain | Residue | Details |
A | GLU167-LEU177 | |
site_id | PS00436 |
Number of Residues | 12 |
Details | PEROXIDASE_2 Peroxidases active site signature. GPvlVRLaWHIS |
Chain | Residue | Details |
A | GLY43-SER54 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | HIS52 | |
Chain | Residue | Details |
A | GLY191 | |
Chain | Residue | Details |
A | HIS175 | |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | ARG48 | |
Chain | Residue | Details |
A | TYR153 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1apx |
Chain | Residue | Details |
A | ARG48 | |
A | HIS52 | |
A | ASN82 | |
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 709 |
Chain | Residue | Details |
A | ARG48 | electrostatic stabiliser |
A | HIS52 | electrostatic stabiliser, proton acceptor, proton donor |
A | GLY191 | single electron acceptor, single electron donor |