1MYG
HIGH RESOLUTION X-RAY STRUCTURES OF PIG METMYOGLOBIN AND TWO CD3 MUTANTS MB(LYS45-> ARG) AND MB(LYS45-> SER)
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 | 0098809 | molecular_function | nitrite reductase activity |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0005344 | molecular_function | oxygen carrier activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0015671 | biological_process | oxygen transport |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016528 | cellular_component | sarcoplasm |
| B | 0019430 | biological_process | removal of superoxide radicals |
| B | 0019825 | molecular_function | oxygen binding |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0098809 | molecular_function | nitrite reductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 300 |
| Chain | Residue |
| B | LYS45 |
| B | LYS63 |
| B | HIS64 |
| B | THR67 |
| B | HOH336 |
| B | HOH399 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 301 |
| Chain | Residue |
| A | THR67 |
| A | HOH351 |
| A | HOH358 |
| A | LYS45 |
| A | LYS63 |
| A | HIS64 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEM A 154 |
| Chain | Residue |
| A | LYS42 |
| A | PHE43 |
| A | LYS45 |
| A | HIS64 |
| A | THR67 |
| A | VAL68 |
| A | LEU89 |
| A | SER92 |
| A | HIS93 |
| A | HIS97 |
| A | ILE99 |
| A | TYR103 |
| A | HOH303 |
| A | HOH351 |
| A | HOH364 |
| A | HOH379 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM B 154 |
| Chain | Residue |
| B | LYS42 |
| B | PHE43 |
| B | LYS45 |
| B | HIS64 |
| B | THR67 |
| B | VAL68 |
| B | ALA71 |
| B | LEU89 |
| B | SER92 |
| B | HIS93 |
| B | HIS97 |
| B | ILE99 |
| B | TYR103 |
| B | PHE138 |
| B | HOH305 |
| B | HOH310 |
| B | HOH378 |
| B | HOH399 |
| B | HOH409 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:9843395, ECO:0007744|PDB:1MNO |
| Chain | Residue | Details |
| A | GLY65 | |
| B | GLY65 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: proximal binding residue => ECO:0000269|PubMed:2383370, ECO:0000269|PubMed:9843395, ECO:0007744|PDB:1M6C, ECO:0007744|PDB:1M6M, ECO:0007744|PDB:1MDN, ECO:0007744|PDB:1MNH, ECO:0007744|PDB:1MNI, ECO:0007744|PDB:1MNJ, ECO:0007744|PDB:1MNK, ECO:0007744|PDB:1MNO, ECO:0007744|PDB:1MWC, ECO:0007744|PDB:1MWD, ECO:0007744|PDB:1MYG, ECO:0007744|PDB:1MYH, ECO:0007744|PDB:1MYI, ECO:0007744|PDB:1MYJ, ECO:0007744|PDB:1PMB, ECO:0007744|PDB:1YCA, ECO:0007744|PDB:1YCB |
| Chain | Residue | Details |
| A | ALA94 | |
| B | ALA94 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9QZ76 |
| Chain | Residue | Details |
| A | ASP4 | |
| B | ASP4 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04247 |
| Chain | Residue | Details |
| A | VAL68 | |
| B | VAL68 |
