2V1I
Crystal structure of radiation-induced metmyoglobin - aqua ferrous myoglobin at pH 6.8
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 | 25 |
Details | BINDING SITE FOR RESIDUE HEM A1154 |
Chain | Residue |
A | THR39 |
A | HIS93 |
A | HIS97 |
A | ILE99 |
A | TYR103 |
A | LEU104 |
A | HIS113 |
A | HIS116 |
A | GLN128 |
A | GOL1158 |
A | HOH2102 |
A | LYS42 |
A | HOH2201 |
A | HOH2202 |
A | HOH2203 |
A | HOH2204 |
A | HOH2205 |
A | HOH2212 |
A | PHE43 |
A | LYS45 |
A | HIS64 |
A | VAL67 |
A | VAL68 |
A | LEU89 |
A | SER92 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A1156 |
Chain | Residue |
A | THR51 |
A | GLU52 |
A | HOH2088 |
A | HOH2206 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A1157 |
Chain | Residue |
A | GLY1 |
A | HOH2208 |
A | HOH2209 |
A | HOH2210 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A1158 |
Chain | Residue |
A | LYS45 |
A | LYS63 |
A | HIS64 |
A | HIS116 |
A | SER117 |
A | HEM1154 |
A | GOL1159 |
A | HOH2152 |
A | HOH2204 |
A | HOH2211 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GOL A1159 |
Chain | Residue |
A | ARG31 |
A | LYS45 |
A | ASP60 |
A | HIS113 |
A | SER117 |
A | GOL1158 |
A | HOH2053 |
A | HOH2098 |
A | HOH2212 |
A | HOH2213 |
A | HOH2214 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A1160 |
Chain | Residue |
A | SER3 |
A | ASP4 |
A | GLY5 |
A | LYS98 |
A | HOH2215 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A1161 |
Chain | Residue |
A | ARG31 |
A | HIS36 |
A | LYS96 |
A | ASP109 |
A | ALA110 |
A | HOH2148 |
A | HOH2217 |
A | HOH2218 |
A | HOH2219 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P02189, ECO:0000255|PROSITE-ProRule:PRU00238 |
Chain | Residue | Details |
A | HIS64 |
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 |