4YU3
The crystal structure of mongoose (Helogale parvula) hemoglobin at pH 8.2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005344 | molecular_function | oxygen carrier activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005833 | cellular_component | hemoglobin complex |
| A | 0015671 | biological_process | oxygen transport |
| A | 0019825 | molecular_function | oxygen binding |
| A | 0020037 | molecular_function | heme binding |
| A | 0031720 | molecular_function | haptoglobin binding |
| A | 0031838 | cellular_component | haptoglobin-hemoglobin complex |
| A | 0042744 | biological_process | hydrogen peroxide catabolic process |
| A | 0043177 | molecular_function | organic acid binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0072562 | cellular_component | blood microparticle |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0005344 | molecular_function | oxygen carrier activity |
| B | 0005833 | cellular_component | hemoglobin complex |
| B | 0015671 | biological_process | oxygen transport |
| B | 0019825 | molecular_function | oxygen binding |
| B | 0020037 | molecular_function | heme binding |
| B | 0031720 | molecular_function | haptoglobin binding |
| B | 0031721 | molecular_function | hemoglobin alpha binding |
| B | 0031838 | cellular_component | haptoglobin-hemoglobin complex |
| B | 0042744 | biological_process | hydrogen peroxide catabolic process |
| B | 0043177 | molecular_function | organic acid binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0072562 | cellular_component | blood microparticle |
| B | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue HEM A 201 |
| Chain | Residue |
| A | TYR42 |
| A | VAL93 |
| A | ASN97 |
| A | PHE98 |
| A | LEU101 |
| A | LEU136 |
| A | OXY202 |
| A | HOH323 |
| A | PHE43 |
| A | HIS45 |
| A | PHE46 |
| A | HIS58 |
| A | LYS61 |
| A | LEU86 |
| A | HIS87 |
| A | LEU91 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue OXY A 202 |
| Chain | Residue |
| A | PHE43 |
| A | HIS58 |
| A | VAL62 |
| A | HEM201 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | binding site for residue HEM B 201 |
| Chain | Residue |
| B | PHE41 |
| B | PHE42 |
| B | PHE45 |
| B | HIS63 |
| B | LYS66 |
| B | SER70 |
| B | PHE71 |
| B | LEU88 |
| B | HIS92 |
| B | LEU96 |
| B | VAL98 |
| B | ASN102 |
| B | LEU106 |
| B | LEU141 |
| B | OXY202 |
| B | HOH311 |
| B | HOH315 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue OXY B 202 |
| Chain | Residue |
| B | HIS63 |
| B | VAL67 |
| B | HIS92 |
| B | HEM201 |
