2E2Y
Crystal Structure of F43W/H64D/V68I Myoglobin
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1001 |
| Chain | Residue |
| A | LYS87 |
| A | GLY124 |
| A | ALA125 |
| A | ASP126 |
| A | HOH1027 |
| A | HOH1092 |
| A | HOH1172 |
| A | HOH1177 |
| A | HOH1205 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1002 |
| Chain | Residue |
| A | SER3 |
| A | GLY5 |
| A | HOH1043 |
| A | HOH1191 |
| A | HOH1213 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1003 |
| Chain | Residue |
| A | SER3 |
| A | GLU4 |
| A | LYS34 |
| A | THR51 |
| A | GLU52 |
| A | ALA53 |
| A | HOH1043 |
| A | HOH1199 |
| A | HOH1200 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM A 154 |
| Chain | Residue |
| A | LYS42 |
| A | TRP43 |
| A | THR67 |
| A | ILE68 |
| A | ALA71 |
| A | LEU89 |
| A | SER92 |
| A | HIS93 |
| A | HIS97 |
| A | ILE99 |
| A | HOH1045 |
| A | HOH1065 |
| A | HOH1074 |
| A | HOH1143 |
| A | HOH1178 |
| A | HOH1194 |
| A | HOH1224 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 600 |
| Chain | Residue |
| A | ALA57 |
| A | SER58 |
| A | GLU59 |
| A | ASP60 |
| A | HOH1112 |
| A | HOH1137 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:7463482, ECO:0007744|PDB:1MBO |
| Chain | Residue | Details |
| A | ASP64 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:845959, ECO:0007744|PDB:4MBN, ECO:0007744|PDB:5MBN |
| Chain | Residue | Details |
| A | HIS93 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9QZ76 |
| Chain | Residue | Details |
| A | SER3 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04247 |
| Chain | Residue | Details |
| A | THR67 |
