1JW8
1.3 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF P6 FORM OF MYOGLOBIN
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005344 | molecular_function | oxygen carrier activity |
| 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 | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 157 |
| Chain | Residue |
| A | SER4 |
| A | GLU5 |
| A | THR52 |
| A | GLU53 |
| A | ALA54 |
| A | HOH1093 |
| A | HOH1227 |
| A | HOH1232 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 158 |
| Chain | Residue |
| A | LYS17 |
| A | LYS17 |
| A | HOH1236 |
| A | HOH1236 |
| A | HOH1236 |
| A | LYS17 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 159 |
| Chain | Residue |
| A | GLY125 |
| A | ALA126 |
| A | ASP127 |
| A | HOH1025 |
| A | HOH1028 |
| A | HOH1166 |
| A | HOH1211 |
| A | HOH1256 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM A 155 |
| Chain | Residue |
| A | THR40 |
| A | LYS43 |
| A | PHE44 |
| A | ARG46 |
| A | HIS65 |
| A | THR68 |
| A | VAL69 |
| A | ALA72 |
| A | LEU90 |
| A | SER93 |
| A | HIS94 |
| A | HIS98 |
| A | ILE100 |
| A | TYR104 |
| A | LEU105 |
| A | CMO156 |
| A | HOH1036 |
| A | HOH1078 |
| A | HOH1081 |
| A | HOH1082 |
| A | HOH1110 |
| A | HOH1136 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CMO A 156 |
| Chain | Residue |
| A | PHE44 |
| A | HIS65 |
| A | VAL69 |
| A | HEM155 |
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 |
