3VRF
The crystal structure of hemoglobin from woolly mammoth in the carbonmonoxy forms
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 | 18 |
| Details | BINDING SITE FOR RESIDUE HEM A 201 |
| Chain | Residue |
| A | TYR42 |
| A | VAL93 |
| A | ASN97 |
| A | PHE98 |
| A | LEU101 |
| A | LEU136 |
| A | CMO202 |
| A | HOH355 |
| A | HOH397 |
| B | HOH318 |
| A | PHE43 |
| A | HIS45 |
| A | PHE46 |
| A | HIS58 |
| A | LYS61 |
| A | LEU86 |
| A | HIS87 |
| A | LEU91 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CMO A 202 |
| Chain | Residue |
| A | HIS58 |
| A | VAL62 |
| A | HEM201 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEM B 201 |
| Chain | Residue |
| B | PHE41 |
| B | PHE42 |
| B | HIS44 |
| B | HIS63 |
| B | SER70 |
| B | LEU88 |
| B | HIS92 |
| B | LEU96 |
| B | ASN102 |
| B | PHE103 |
| B | LEU106 |
| B | LEU141 |
| B | CMO202 |
| B | HOH353 |
| B | HOH385 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CMO B 202 |
| Chain | Residue |
| B | PHE42 |
| B | HIS63 |
| B | VAL67 |
| B | HEM201 |
