Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004096 | molecular_function | catalase activity |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0020037 | molecular_function | heme binding |
| B | 0004096 | molecular_function | catalase activity |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0020037 | molecular_function | heme binding |
| C | 0004096 | molecular_function | catalase activity |
| C | 0006979 | biological_process | response to oxidative stress |
| C | 0020037 | molecular_function | heme binding |
| D | 0004096 | molecular_function | catalase activity |
| D | 0006979 | biological_process | response to oxidative stress |
| D | 0020037 | molecular_function | heme binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM A 4000 |
| Chain | Residue |
| A | ARG99 |
| A | PHE180 |
| A | PHE188 |
| A | ILE248 |
| A | HIS249 |
| A | PHE365 |
| A | LEU381 |
| A | ARG385 |
| A | SER388 |
| A | TYR389 |
| A | THR392 |
| A | VAL100 |
| A | GLN393 |
| A | ARG396 |
| D | LEU88 |
| A | VAL101 |
| A | HIS102 |
| A | ARG139 |
| A | GLY158 |
| A | VAL173 |
| A | GLY174 |
| A | ASN175 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM B 4000 |
| Chain | Residue |
| B | ARG99 |
| B | VAL100 |
| B | VAL101 |
| B | HIS102 |
| B | ARG139 |
| B | VAL173 |
| B | GLY174 |
| B | ASN175 |
| B | PHE180 |
| B | ALA185 |
| B | PHE188 |
| B | ILE248 |
| B | HIS249 |
| B | PHE365 |
| B | LEU381 |
| B | ARG385 |
| B | SER388 |
| B | TYR389 |
| B | GLN393 |
| B | ARG396 |
| C | ASP92 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM C 4000 |
| Chain | Residue |
| B | LEU88 |
| C | ARG99 |
| C | VAL100 |
| C | VAL101 |
| C | HIS102 |
| C | ARG139 |
| C | GLY158 |
| C | VAL173 |
| C | GLY174 |
| C | ASN175 |
| C | PHE180 |
| C | ALA185 |
| C | PHE188 |
| C | ILE248 |
| C | HIS249 |
| C | PHE365 |
| C | LEU381 |
| C | ARG385 |
| C | SER388 |
| C | TYR389 |
| C | THR392 |
| C | GLN393 |
| C | ARG396 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM D 4000 |
| Chain | Residue |
| A | LEU88 |
| A | ASP92 |
| D | ARG99 |
| D | VAL101 |
| D | HIS102 |
| D | ARG139 |
| D | VAL173 |
| D | GLY174 |
| D | ASN175 |
| D | PHE180 |
| D | ALA185 |
| D | PHE188 |
| D | ILE248 |
| D | HIS249 |
| D | PHE365 |
| D | LEU381 |
| D | ARG385 |
| D | SER388 |
| D | TYR389 |
| D | THR392 |
| D | GLN393 |
| D | ARG396 |
Functional Information from PROSITE/UniProt
| site_id | PS00438 |
| Number of Residues | 17 |
| Details | CATALASE_2 Catalase proximal active site signature. FdHeripERvvHarGAG |
| Chain | Residue | Details |
| A | PHE91-GLY107 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10013","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000250"}]} |
