1BZ6
ATOMIC RESOLUTION CRYSTAL STRUCTURE AQUOMET-MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATURE
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 | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 201 |
| Chain | Residue |
| A | SER58 |
| A | GLU59 |
| A | ASP60 |
| A | HOH368 |
| A | HOH376 |
| A | HOH401 |
| A | HOH479 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 202 |
| Chain | Residue |
| A | ASP122 |
| A | HOH343 |
| A | PRO120 |
| A | GLY121 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 203 |
| Chain | Residue |
| A | ARG45 |
| A | LYS63 |
| A | HIS64 |
| A | THR67 |
| A | HIS116 |
| A | HOH348 |
| A | HOH354 |
| A | HOH355 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 204 |
| Chain | Residue |
| A | ARG31 |
| A | SER35 |
| A | LYS96 |
| A | GLU109 |
| A | HOH301 |
| A | HOH315 |
| A | HOH430 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM A 154 |
| Chain | Residue |
| A | LYS42 |
| A | PHE43 |
| A | ARG45 |
| A | HIS64 |
| A | THR67 |
| A | VAL68 |
| A | LEU89 |
| A | SER92 |
| A | HIS93 |
| A | HIS97 |
| A | ILE99 |
| A | TYR103 |
| A | HOH305 |
| A | HOH355 |
| A | HOH378 |
| A | HOH384 |
| A | HOH389 |
| A | HOH406 |
| A | HOH440 |
| A | HOH480 |
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 | GLY65 |
| 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 | ALA94 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9QZ76 |
| Chain | Residue | Details |
| A | GLU4 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04247 |
| Chain | Residue | Details |
| A | VAL68 |
