5UC8
Crystal structure of human Heme Oxygenase-2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004392 | molecular_function | heme oxygenase (decyclizing) activity |
| A | 0006788 | biological_process | heme oxidation |
| B | 0004392 | molecular_function | heme oxygenase (decyclizing) activity |
| B | 0006788 | biological_process | heme oxidation |
| C | 0004392 | molecular_function | heme oxygenase (decyclizing) activity |
| C | 0006788 | biological_process | heme oxidation |
| D | 0004392 | molecular_function | heme oxygenase (decyclizing) activity |
| D | 0006788 | biological_process | heme oxidation |
Functional Information from PROSITE/UniProt
| site_id | PS00593 |
| Number of Residues | 11 |
| Details | HEME_OXYGENASE Heme oxygenase signature. LVAHAYTRYMG |
| Chain | Residue | Details |
| A | LEU149-GLY159 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"17965015","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2QPP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17965015","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2QPP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"P09601","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
