1NAZ
structure of microgravity-grown oxidized myoglobin mutant YQR (ISS8A)
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 | 4 |
| Details | BINDING SITE FOR RESIDUE OH A 500 |
| Chain | Residue |
| A | TYR29 |
| A | GLN64 |
| A | VAL68 |
| A | HEM200 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 413 |
| Chain | Residue |
| A | HOH600 |
| A | HOH679 |
| A | HOH693 |
| A | HOH771 |
| A | HOH780 |
| A | SER3 |
| A | GLU4 |
| A | THR51 |
| A | GLU52 |
| A | ALA53 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 414 |
| Chain | Residue |
| A | SER3 |
| A | GLY5 |
| A | HOH661 |
| A | HOH679 |
| A | HOH716 |
| A | HOH771 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 415 |
| Chain | Residue |
| A | GLY124 |
| A | ALA125 |
| A | ASP126 |
| A | HOH522 |
| A | HOH611 |
| A | HOH707 |
| A | HOH758 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEM A 200 |
| Chain | Residue |
| A | THR39 |
| A | LYS42 |
| A | PHE43 |
| A | ARG45 |
| A | GLN64 |
| A | ARG67 |
| A | VAL68 |
| A | LEU89 |
| A | SER92 |
| A | HIS93 |
| A | HIS97 |
| A | ILE99 |
| A | TYR103 |
| A | LEU104 |
| A | OH500 |
| A | HOH532 |
| A | HOH539 |
| A | HOH581 |
| A | HOH615 |
| A | HOH685 |
| A | HOH727 |
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 | GLN64 |
| 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 | ARG67 |
