6IYH
X-ray sequence and high resolution crystal structure of Persian sturgeon methemoglobin
Replaces: 5JGGFunctional 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 | 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 | 19 |
| Details | binding site for residue HEM A 201 |
| Chain | Residue |
| A | MET33 |
| A | HIS89 |
| A | LEU93 |
| A | VAL95 |
| A | ASN99 |
| A | LEU103 |
| A | LEU138 |
| A | HOH324 |
| A | HOH357 |
| A | HOH363 |
| A | HOH393 |
| A | TYR43 |
| A | PHE44 |
| A | HIS46 |
| A | TYR47 |
| A | HIS60 |
| A | LYS63 |
| A | LEU85 |
| A | LEU88 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue HEM B 201 |
| Chain | Residue |
| B | TYR41 |
| B | PHE42 |
| B | HIS63 |
| B | LEU88 |
| B | HIS92 |
| B | LEU96 |
| B | ASN102 |
| B | PHE103 |
| B | PHE106 |
| B | LEU141 |
| B | HOH309 |
| B | HOH314 |
| B | HOH334 |
| B | HOH350 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue PGO B 202 |
| Chain | Residue |
| A | PHE37 |
| A | ILE102 |
| B | ASP108 |
| B | HOH354 |
| B | HOH390 |
