1FHJ
CRYSTAL STRUCTURE OF AQUOMET HEMOGLOBIN-I OF THE MANED WOLF (CHRYSOCYON BRACHYURUS) AT 2.0 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 |
| 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 |
| C | 0004601 | molecular_function | peroxidase activity |
| C | 0005344 | molecular_function | oxygen carrier activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0005833 | cellular_component | hemoglobin complex |
| C | 0015671 | biological_process | oxygen transport |
| C | 0019825 | molecular_function | oxygen binding |
| C | 0020037 | molecular_function | heme binding |
| C | 0031720 | molecular_function | haptoglobin binding |
| C | 0031838 | cellular_component | haptoglobin-hemoglobin complex |
| C | 0042744 | biological_process | hydrogen peroxide catabolic process |
| C | 0043177 | molecular_function | organic acid binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0072562 | cellular_component | blood microparticle |
| D | 0004601 | molecular_function | peroxidase activity |
| D | 0005344 | molecular_function | oxygen carrier activity |
| D | 0005833 | cellular_component | hemoglobin complex |
| D | 0015671 | biological_process | oxygen transport |
| D | 0019825 | molecular_function | oxygen binding |
| D | 0020037 | molecular_function | heme binding |
| D | 0031720 | molecular_function | haptoglobin binding |
| D | 0031721 | molecular_function | hemoglobin alpha binding |
| D | 0031838 | cellular_component | haptoglobin-hemoglobin complex |
| D | 0042744 | biological_process | hydrogen peroxide catabolic process |
| D | 0043177 | molecular_function | organic acid binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0072562 | cellular_component | blood microparticle |
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 | PHE98 |
| A | LEU136 |
| A | HOH191 |
| A | HOH193 |
| A | PHE43 |
| A | HIS45 |
| A | HIS58 |
| A | LYS61 |
| A | HIS87 |
| A | LEU91 |
| A | VAL93 |
| A | ASN97 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM B 147 |
| Chain | Residue |
| B | ALA5 |
| B | PHE41 |
| B | PHE42 |
| B | HIS63 |
| B | LYS66 |
| B | SER70 |
| B | HIS92 |
| B | LEU96 |
| B | VAL98 |
| B | ASN102 |
| B | LEU106 |
| B | LEU141 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEM C 142 |
| Chain | Residue |
| C | TYR42 |
| C | PHE43 |
| C | HIS45 |
| C | HIS58 |
| C | LYS61 |
| C | LEU83 |
| C | HIS87 |
| C | LEU91 |
| C | VAL93 |
| C | ASN97 |
| C | PHE98 |
| C | LEU136 |
| C | HOH183 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM D 147 |
| Chain | Residue |
| D | PHE41 |
| D | LYS59 |
| D | HIS63 |
| D | LYS66 |
| D | SER70 |
| D | HIS92 |
| D | LEU96 |
| D | ASN102 |
| D | PHE103 |
| D | LEU106 |
| D | LEU141 |
| D | HOH190 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: distal binding residue |
| Chain | Residue | Details |
| B | HIS63 | |
| D | HIS63 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: proximal binding residue |
| Chain | Residue | Details |
| B | HIS92 | |
| D | HIS92 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylvaline => ECO:0000250|UniProtKB:P02086 |
| Chain | Residue | Details |
| B | VAL1 | |
| D | VAL1 | |
| A | SER49 | |
| C | SER3 | |
| C | SER35 | |
| C | SER49 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68871 |
| Chain | Residue | Details |
| B | SER44 | |
| D | SER44 | |
| A | LYS40 | |
| C | LYS7 | |
| C | LYS11 | |
| C | LYS40 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P68871 |
| Chain | Residue | Details |
| B | LYS59 | |
| B | LYS82 | |
| B | LYS144 | |
| D | LYS59 | |
| D | LYS82 | |
| D | LYS144 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P68871 |
| Chain | Residue | Details |
| B | CYS93 | |
| D | CYS93 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P69905 |
| Chain | Residue | Details |
| A | TYR24 | |
| C | TYR24 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P01942 |
| Chain | Residue | Details |
| A | SER102 | |
| A | SER124 | |
| A | SER138 | |
| C | SER102 | |
| C | SER124 | |
| C | SER138 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P01942 |
| Chain | Residue | Details |
| A | THR108 | |
| A | THR134 | |
| A | THR137 | |
| C | THR108 | |
| C | THR134 | |
| C | THR137 |
