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 PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2011 |
| Chain | Residue |
| B | HOH40 |
| B | LYS470 |
| B | LYS473 |
| B | ARG477 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2012 |
| Chain | Residue |
| B | VAL382 |
| B | ARG385 |
| B | GLY459 |
| B | HOH1040 |
| B | HOH1216 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2013 |
| Chain | Residue |
| A | SER26 |
| A | THR27 |
| A | HIS205 |
| A | HOH2067 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 C 2014 |
| Chain | Residue |
| C | ARG745 |
| C | ARG749 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 2015 |
| Chain | Residue |
| C | VAL682 |
| C | ARG685 |
| C | GLY759 |
| C | GLU764 |
| C | HOH1103 |
| C | HOH1155 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEM A 901 |
| Chain | Residue |
| A | LYS13 |
| A | HIS20 |
| A | ALA23 |
| A | TYR130 |
| A | VAL131 |
| A | GLY135 |
| A | SER138 |
| A | ARG177 |
| A | PHE201 |
| A | ASN204 |
| A | PHE208 |
| A | HOH2062 |
| A | HOH2070 |
| A | HOH2072 |
| A | HOH2075 |
| A | HOH2078 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM B 902 |
| Chain | Residue |
| B | HOH114 |
| B | LYS313 |
| B | HIS320 |
| B | ALA323 |
| B | GLU324 |
| B | MET329 |
| B | LEU333 |
| B | TYR430 |
| B | VAL431 |
| B | GLY435 |
| B | SER438 |
| B | VAL442 |
| B | ARG477 |
| B | PHE501 |
| B | ASN504 |
| B | PHE508 |
| B | HOH1035 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM C 903 |
| Chain | Residue |
| C | HOH8 |
| C | HOH93 |
| C | LYS613 |
| C | HIS620 |
| C | ALA623 |
| C | GLU624 |
| C | LEU633 |
| C | TYR730 |
| C | VAL731 |
| C | GLY735 |
| C | SER738 |
| C | ARG777 |
| C | ASN804 |
| C | HOH1039 |
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 | ALA136 | |
| A | GLY140 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1wnw |
| Chain | Residue | Details |
| B | GLY440 | |
| B | ALA436 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1wnw |
| Chain | Residue | Details |
| C | GLY740 | |
| C | ALA736 | |
| 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 | ALA136 | 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 | ALA436 | 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 | ALA736 | modifies pKa |
| C | GLY740 | steric role |
