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: axial binding residue => ECO:0000250 |
Chain | Residue | Details |
A | HIS20 | |
B | HIS320 | |
C | HIS620 | |
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 |