1S0H
Structure determination of haemoglobin from Donkey(equus asinus) at 3.0 Angstrom resolution
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 | 13 |
| Details | BINDING SITE FOR RESIDUE HEM A 142 |
| Chain | Residue |
| A | TYR42 |
| A | VAL93 |
| A | ASN97 |
| A | PHE98 |
| A | LEU136 |
| A | PHE43 |
| A | HIS45 |
| A | LYS61 |
| A | ALA65 |
| A | LEU83 |
| A | LEU86 |
| A | HIS87 |
| A | LEU91 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM B 147 |
| Chain | Residue |
| B | THR38 |
| B | PHE41 |
| B | PHE42 |
| B | HIS63 |
| B | SER70 |
| B | PHE85 |
| B | LEU88 |
| B | LEU91 |
| B | HIS92 |
| B | LEU96 |
| B | PHE103 |
| B | LEU141 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00238 |
| Chain | Residue | Details |
| A | GLY59 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238 |
| Chain | Residue | Details |
| A | ALA88 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P69905 |
| Chain | Residue | Details |
| A | ALA4 | |
| A | HIS50 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P01942 |
| Chain | Residue | Details |
| A | THR8 | |
| A | ALA12 | |
| A | THR41 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P69905 |
| Chain | Residue | Details |
| A | ASN9 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P01942 |
| Chain | Residue | Details |
| A | VAL17 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P01942 |
| Chain | Residue | Details |
| A | HIS103 | |
| A | LEU125 | |
| A | LYS139 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P01942 |
| Chain | Residue | Details |
| A | LEU109 | |
| A | VAL135 | |
| A | SER138 |
