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 |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0020037 | molecular_function | heme binding |
| B | 0034599 | biological_process | cellular response to oxidative stress |
| C | 0004601 | molecular_function | peroxidase activity |
| C | 0006979 | biological_process | response to oxidative stress |
| C | 0020037 | molecular_function | heme binding |
| C | 0034599 | biological_process | cellular response to oxidative stress |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue HEM A 301 |
| Chain | Residue |
| A | PRO44 |
| A | GLY178 |
| A | LYS179 |
| A | THR180 |
| A | HIS181 |
| A | ASN184 |
| A | SER185 |
| A | TRP191 |
| A | LEU232 |
| A | HOH436 |
| A | HOH439 |
| A | VAL45 |
| A | HOH459 |
| A | HOH502 |
| A | ARG48 |
| A | TRP51 |
| A | PRO145 |
| A | ASP146 |
| A | LEU171 |
| A | ALA174 |
| A | MHS175 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CO A 302 |
| Chain | Residue |
| A | HIS0 |
| A | HIS2 |
| A | HIS60 |
| A | HOH524 |
| A | HOH585 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MN A 303 |
| Chain | Residue |
| A | HIS1 |
| A | HIS3 |
| A | HOH441 |
| A | HOH564 |
| C | ASP34 |
| C | HOH411 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue NA A 304 |
| Chain | Residue |
| A | ASP34 |
| A | HOH407 |
| A | HOH533 |
| B | HIS1 |
| B | HIS3 |
| B | NA301 |
| B | HOH503 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue NA B 301 |
| Chain | Residue |
| A | ASP34 |
| A | NA304 |
| A | HOH407 |
| A | HOH533 |
| B | HIS1 |
| B | HIS3 |
| B | HOH503 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | binding site for residue HEM B 302 |
| Chain | Residue |
| B | PRO44 |
| B | VAL45 |
| B | ARG48 |
| B | TRP51 |
| B | PRO145 |
| B | ASP146 |
| B | LEU171 |
| B | ALA174 |
| B | MHS175 |
| B | GLY178 |
| B | LYS179 |
| B | THR180 |
| B | HIS181 |
| B | ASN184 |
| B | SER185 |
| B | TRP191 |
| B | LEU232 |
| B | HOH415 |
| B | HOH422 |
| B | HOH461 |
| B | HOH470 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue CO B 303 |
| Chain | Residue |
| B | HIS-1 |
| B | HIS-2 |
| B | HOH588 |
| B | HOH589 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue CO B 304 |
| Chain | Residue |
| B | HIS0 |
| B | HIS2 |
| B | HIS60 |
| B | HOH534 |
| B | HOH550 |
| B | HOH561 |
| site_id | AC9 |
| Number of Residues | 22 |
| Details | binding site for residue HEM C 301 |
| Chain | Residue |
| C | PRO44 |
| C | VAL45 |
| C | ARG48 |
| C | TRP51 |
| C | PRO145 |
| C | ASP146 |
| C | LEU171 |
| C | ALA174 |
| C | MHS175 |
| C | GLY178 |
| C | LYS179 |
| C | THR180 |
| C | HIS181 |
| C | ASN184 |
| C | SER185 |
| C | TRP191 |
| C | LEU232 |
| C | HOH402 |
| C | HOH410 |
| C | HOH412 |
| C | HOH418 |
| C | HOH449 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue CO C 302 |
| Chain | Residue |
| B | ASP34 |
| B | HOH407 |
| B | HOH546 |
| B | HOH547 |
| C | HIS1 |
| C | HIS3 |
| C | HOH405 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue CO C 303 |
| Chain | Residue |
| C | HIS0 |
| C | HIS2 |
| C | HIS60 |
| C | HOH488 |
| C | HOH568 |
| C | HOH570 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue CO C 304 |
| Chain | Residue |
| B | HOH624 |
| C | HIS-1 |
| C | HIS-2 |
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. GPvlVRLaWHTS |
| Chain | Residue | Details |
| A | GLY43-SER54 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | HIS52 | |
| B | HIS52 | |
| C | HIS52 | |
| Chain | Residue | Details |
| A | TRP191 | |
| B | TRP191 | |
| C | TRP191 | |
| Chain | Residue | Details |
| A | MHS175 | |
| B | MHS175 | |
| C | MHS175 | |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| A | ARG48 | |
| B | ARG48 | |
| C | ARG48 | |
| Chain | Residue | Details |
| A | TYR153 | |
| B | TYR153 | |
| C | TYR153 | |
Catalytic Information from CSA
| 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 | TRP191 | single electron acceptor, single electron donor |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 709 |
| Chain | Residue | Details |
| B | ARG48 | electrostatic stabiliser |
| B | HIS52 | electrostatic stabiliser, proton acceptor, proton donor |
| B | TRP191 | single electron acceptor, single electron donor |
| site_id | MCSA3 |
| Number of Residues | 3 |
| Details | M-CSA 709 |
| Chain | Residue | Details |
| C | ARG48 | electrostatic stabiliser |
| C | HIS52 | electrostatic stabiliser, proton acceptor, proton donor |
| C | TRP191 | single electron acceptor, single electron donor |
