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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 701 |
| Chain | Residue |
| A | ASN91 |
| A | SER93 |
| A | GLU95 |
| A | TRP96 |
| A | ARG99 |
| A | HOH1049 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 702 |
| Chain | Residue |
| A | HOH931 |
| A | HOH1095 |
| A | SER26 |
| A | THR27 |
| A | HIS205 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 703 |
| Chain | Residue |
| B | SER26 |
| B | THR27 |
| B | HIS205 |
| B | HOH932 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 705 |
| Chain | Residue |
| A | SER138 |
| A | LYS173 |
| A | ARG177 |
| A | HOH1009 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 706 |
| Chain | Residue |
| A | ARG112 |
| A | HIS192 |
| A | HOH941 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE YOM A 901 |
| Chain | Residue |
| A | HIS20 |
| A | GLU24 |
| A | VAL131 |
| A | ARG132 |
| A | LEU134 |
| A | GLY135 |
| A | SER138 |
| A | GLY139 |
| A | PHE201 |
| A | ASN204 |
| A | PHE208 |
| A | HOH1054 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE YOM B 902 |
| Chain | Residue |
| B | HIS20 |
| B | GLU24 |
| B | VAL131 |
| B | GLY135 |
| B | SER138 |
| B | GLY139 |
| B | PHE201 |
| B | ASN204 |
| B | PHE208 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 801 |
| Chain | Residue |
| A | VAL39 |
| A | TYR151 |
| B | ASN119 |
| B | ASP121 |
| B | HIS192 |
| B | GLU196 |
| B | HOH1024 |
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 | 2 |
| 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 | ASP136 | |
| B | GLY140 | |
| 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 | HIS25 | metal ligand |
| B | TYR53 | activator, electrostatic stabiliser |
| B | VAL131 | activator |
| B | ARG132 | activator |
| B | GLY135 | steric role |
| B | ASP136 | modifies pKa |
| B | GLY140 | steric role |
