3RJ6
Crystal Structure of Horse heart ferric myoglobin; K45E/K63E/K96E mutant
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004601 | molecular_function | peroxidase activity |
A | 0005344 | molecular_function | oxygen carrier activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0015671 | biological_process | oxygen transport |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016528 | cellular_component | sarcoplasm |
A | 0019430 | biological_process | removal of superoxide radicals |
A | 0019825 | molecular_function | oxygen binding |
A | 0020037 | molecular_function | heme binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0098809 | molecular_function | nitrite reductase activity |
B | 0004601 | molecular_function | peroxidase activity |
B | 0005344 | molecular_function | oxygen carrier activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0015671 | biological_process | oxygen transport |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016528 | cellular_component | sarcoplasm |
B | 0019430 | biological_process | removal of superoxide radicals |
B | 0019825 | molecular_function | oxygen binding |
B | 0020037 | molecular_function | heme binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0098809 | molecular_function | nitrite reductase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEM A 154 |
Chain | Residue |
A | THR39 |
A | HIS93 |
A | HIS97 |
A | ILE99 |
A | TYR103 |
A | HIS113 |
A | HIS116 |
A | GLN128 |
A | PHE138 |
A | HOH198 |
A | HOH258 |
A | LYS42 |
A | PHE43 |
A | GLU45 |
A | HIS64 |
A | VAL67 |
A | VAL68 |
A | LEU89 |
A | SER92 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 155 |
Chain | Residue |
A | HIS81 |
A | HIS82 |
A | GLU83 |
A | HOH171 |
B | GLY1 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEM B 154 |
Chain | Residue |
B | THR39 |
B | LYS42 |
B | PHE43 |
B | HIS64 |
B | VAL67 |
B | VAL68 |
B | LEU89 |
B | SER92 |
B | HIS93 |
B | HIS97 |
B | ILE99 |
B | TYR103 |
B | HIS113 |
B | HIS116 |
B | GLN128 |
B | PHE138 |
B | HOH181 |
B | HOH221 |
B | HOH226 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 155 |
Chain | Residue |
A | GLY1 |
B | HIS81 |
B | HIS82 |
B | GLU83 |
B | HOH229 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P02189, ECO:0000255|PROSITE-ProRule:PRU00238 |
Chain | Residue | Details |
A | HIS64 | |
B | HIS64 |
Chain | Residue | Details |
A | HIS93 | |
B | HIS93 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9QZ76 |
Chain | Residue | Details |
A | SER3 | |
B | SER3 |