3ASE
Crystal Structure of Zinc myoglobin soaked with Ru3O cluster
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 | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 200 |
| Chain | Residue |
| A | SER3 |
| A | GLU4 |
| A | THR51 |
| A | GLU52 |
| A | ALA53 |
| A | HOH192 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 201 |
| Chain | Residue |
| A | ASP126 |
| A | HOH169 |
| A | LYS87 |
| A | GLY124 |
| A | ALA125 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE RUO A 154 |
| Chain | Residue |
| A | HIS12 |
| A | HOH216 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE RUO A 155 |
| Chain | Residue |
| A | HIS48 |
| A | HIS81 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ZNH A 156 |
| Chain | Residue |
| A | LYS42 |
| A | PHE43 |
| A | ARG45 |
| A | HIS64 |
| A | THR67 |
| A | VAL68 |
| A | ALA71 |
| A | LEU89 |
| A | SER92 |
| A | HIS93 |
| A | HIS97 |
| A | ILE99 |
| A | TYR103 |
| A | LEU104 |
| A | ILE107 |
| A | PHE138 |
| A | HOH178 |
| A | HOH180 |
| A | HOH191 |
| A | HOH204 |
| A | HOH210 |
| A | HOH224 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 146 |
| Details | Domain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7463482","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MBO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"845959","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MBN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MBN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9QZ76","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P04247","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
