Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004096 | molecular_function | catalase activity |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0020037 | molecular_function | heme binding |
| A | 0042542 | biological_process | response to hydrogen peroxide |
| A | 0042744 | biological_process | hydrogen peroxide catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004096 | molecular_function | catalase activity |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0020037 | molecular_function | heme binding |
| B | 0042542 | biological_process | response to hydrogen peroxide |
| B | 0042744 | biological_process | hydrogen peroxide catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE AZI B 2600 |
| Chain | Residue |
| A | ARG47 |
| A | ARG344 |
| B | ARG47 |
| B | TYR345 |
| B | HOH3091 |
| B | HOH3103 |
| site_id | AC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE HEM A 550 |
| Chain | Residue |
| A | VAL55 |
| A | HIS56 |
| A | ARG93 |
| A | GLY112 |
| A | PHE113 |
| A | ALA114 |
| A | VAL127 |
| A | GLY128 |
| A | ASN129 |
| A | ALA139 |
| A | PHE142 |
| A | SER198 |
| A | HIS199 |
| A | PHE315 |
| A | MET331 |
| A | ARG335 |
| A | SER338 |
| A | TYR339 |
| A | THR342 |
| A | HIS343 |
| A | ARG346 |
| A | OXY1600 |
| A | HOH1606 |
| A | HOH1629 |
| A | HOH1667 |
| A | ASP46 |
| A | ARG53 |
| A | VAL54 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE HEM B 550 |
| Chain | Residue |
| B | LEU42 |
| B | ASP46 |
| B | ARG53 |
| B | VAL54 |
| B | VAL55 |
| B | HIS56 |
| B | ARG93 |
| B | GLY112 |
| B | PHE113 |
| B | ALA114 |
| B | VAL127 |
| B | GLY128 |
| B | ASN129 |
| B | ALA139 |
| B | PHE142 |
| B | GLY197 |
| B | SER198 |
| B | HIS199 |
| B | PHE315 |
| B | MET331 |
| B | ARG335 |
| B | SER338 |
| B | TYR339 |
| B | THR342 |
| B | HIS343 |
| B | ARG346 |
| B | HOH2603 |
| B | HOH2609 |
| B | HOH2657 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE OXY A 1600 |
| Chain | Residue |
| A | HIS56 |
| A | PHE142 |
| A | TYR339 |
| A | HEM550 |
| A | HOH2054 |
Functional Information from PROSITE/UniProt
| site_id | PS00437 |
| Number of Residues | 9 |
| Details | CATALASE_1 Catalase proximal heme-ligand signature. RLFSYgDTH |
| Chain | Residue | Details |
| A | ARG335-HIS343 | |
| site_id | PS00438 |
| Number of Residues | 17 |
| Details | CATALASE_2 Catalase proximal active site signature. FdReripERvvHakGSG |
| Chain | Residue | Details |
| A | PHE45-GLY61 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS56 | |
| A | ASN129 | |
| B | HIS56 | |
| B | ASN129 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue => ECO:0000250 |
| Chain | Residue | Details |
| A | TYR339 | |
| B | TYR339 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1iph |
| Chain | Residue | Details |
| A | HIS56 | |
| A | SER95 | |
| A | ASN129 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1iph |
| Chain | Residue | Details |
| B | HIS56 | |
| B | SER95 | |
| B | ASN129 | |
