Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004392 | molecular_function | heme oxygenase (decyclizing) activity |
| A | 0006788 | biological_process | heme oxidation |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0042167 | biological_process | heme catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004392 | molecular_function | heme oxygenase (decyclizing) activity |
| B | 0006788 | biological_process | heme oxidation |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0042167 | biological_process | heme catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004392 | molecular_function | heme oxygenase (decyclizing) activity |
| C | 0006788 | biological_process | heme oxidation |
| C | 0006979 | biological_process | response to oxidative stress |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0020037 | molecular_function | heme binding |
| C | 0042167 | biological_process | heme catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00593 |
| Number of Residues | 11 |
| Details | HEME_OXYGENASE Heme oxygenase signature. LVAHHYVRYLG |
| Chain | Residue | Details |
| A | LEU125-GLY135 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1wnw |
| Chain | Residue | Details |
| A | ASP136 | |
| A | GLY140 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1wnw |
| Chain | Residue | Details |
| B | GLY440 | |
| B | ASP436 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1wnw |
| Chain | Residue | Details |
| C | GLY740 | |
| C | ASP736 | |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 795 |
| Chain | Residue | Details |
| A | HIS25 | metal ligand |
| A | TYR53 | activator, electrostatic stabiliser |
| A | VAL131 | activator |
| A | ARG132 | activator |
| A | GLY135 | steric role |
| A | ASP136 | modifies pKa |
| A | GLY140 | steric role |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 795 |
| Chain | Residue | Details |
| B | HIS325 | metal ligand |
| B | TYR353 | activator, electrostatic stabiliser |
| B | VAL431 | activator |
| B | ARG432 | activator |
| B | GLY435 | steric role |
| B | ASP436 | modifies pKa |
| B | GLY440 | steric role |
| site_id | MCSA3 |
| Number of Residues | 7 |
| Details | M-CSA 795 |
| Chain | Residue | Details |
| C | HIS625 | metal ligand |
| C | TYR653 | activator, electrostatic stabiliser |
| C | VAL731 | activator |
| C | ARG732 | activator |
| C | GLY735 | steric role |
| C | ASP736 | modifies pKa |
| C | GLY740 | steric role |
