5YCI
Ancestral myoglobin aMbWb' of Basilosaurus relative (polyphyly)
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 | 0070062 | cellular_component | extracellular exosome |
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 | 0070062 | cellular_component | extracellular exosome |
B | 0098809 | molecular_function | nitrite reductase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | binding site for residue HEM A 201 |
Chain | Residue |
A | THR39 |
A | HIS97 |
A | ILE99 |
A | TYR103 |
A | HOH309 |
A | HOH326 |
A | HOH376 |
A | HOH385 |
A | LYS42 |
A | PHE43 |
A | HIS64 |
A | THR67 |
A | VAL68 |
A | LEU89 |
A | SER92 |
A | HIS93 |
site_id | AC2 |
Number of Residues | 19 |
Details | binding site for residue HEM B 201 |
Chain | Residue |
B | THR39 |
B | LYS42 |
B | PHE43 |
B | HIS64 |
B | THR67 |
B | VAL68 |
B | ALA71 |
B | LEU89 |
B | SER92 |
B | HIS93 |
B | HIS97 |
B | ILE99 |
B | TYR103 |
B | HOH301 |
B | HOH325 |
B | HOH339 |
B | HOH340 |
B | HOH347 |
B | HOH351 |
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 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: proximal binding residue => ECO:0000269|PubMed:30442991, ECO:0007744|PDB:5YCI |
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 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04247 |
Chain | Residue | Details |
A | THR67 | |
B | THR67 |