9FY4
Crystal structure of Heme-Oxygenase mutant I143K from Corynebacterium diphtheriae complexed with Cobalt-porphyrine (HumO-Co(III))
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 |
| H | 0004392 | molecular_function | heme oxygenase (decyclizing) activity |
| H | 0006788 | biological_process | heme oxidation |
| H | 0006979 | biological_process | response to oxidative stress |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0020037 | molecular_function | heme binding |
| H | 0042167 | biological_process | heme catabolic process |
| H | 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 |
Catalytic Information from CSA






