1IDR
CRYSTAL STRUCTURE OF THE TRUNCATED-HEMOGLOBIN-N FROM MYCOBACTERIUM TUBERCULOSIS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005344 | molecular_function | oxygen carrier activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008379 | molecular_function | thioredoxin peroxidase activity |
| A | 0008941 | molecular_function | nitric oxide dioxygenase NAD(P)H activity |
| A | 0015671 | biological_process | oxygen transport |
| A | 0019825 | molecular_function | oxygen binding |
| A | 0020037 | molecular_function | heme binding |
| A | 0034599 | biological_process | cellular response to oxidative stress |
| A | 0045454 | biological_process | cell redox homeostasis |
| A | 0046210 | biological_process | nitric oxide catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051410 | biological_process | detoxification of nitrogen compound |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0005344 | molecular_function | oxygen carrier activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008379 | molecular_function | thioredoxin peroxidase activity |
| B | 0008941 | molecular_function | nitric oxide dioxygenase NAD(P)H activity |
| B | 0015671 | biological_process | oxygen transport |
| B | 0019825 | molecular_function | oxygen binding |
| B | 0020037 | molecular_function | heme binding |
| B | 0034599 | biological_process | cellular response to oxidative stress |
| B | 0045454 | biological_process | cell redox homeostasis |
| B | 0046210 | biological_process | nitric oxide catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051410 | biological_process | detoxification of nitrogen compound |
| B | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 A 301 |
| Chain | Residue |
| A | ARG53 |
| A | LYS57 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 A 302 |
| Chain | Residue |
| A | PRO108 |
| A | SER109 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 B 303 |
| Chain | Residue |
| B | GLN82 |
| B | GLY83 |
| B | HOH382 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM A 144 |
| Chain | Residue |
| A | THR49 |
| A | ARG53 |
| A | LEU54 |
| A | GLN58 |
| A | PHE61 |
| A | TYR72 |
| A | GLY74 |
| A | ALA75 |
| A | MET77 |
| A | VAL80 |
| A | HIS81 |
| A | ARG84 |
| A | ILE86 |
| A | PHE91 |
| A | VAL94 |
| A | OXY145 |
| A | HOH382 |
| A | HOH397 |
| A | PHE45 |
| A | PHE46 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM B 144 |
| Chain | Residue |
| B | LEU42 |
| B | PHE45 |
| B | PHE46 |
| B | ARG53 |
| B | LEU54 |
| B | GLN58 |
| B | PHE61 |
| B | TYR72 |
| B | GLY74 |
| B | ALA75 |
| B | MET77 |
| B | VAL80 |
| B | HIS81 |
| B | ILE86 |
| B | HIS90 |
| B | PHE91 |
| B | VAL94 |
| B | ILE119 |
| B | OXY145 |
| B | HOH355 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE OXY A 145 |
| Chain | Residue |
| A | TYR33 |
| A | HEM144 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE OXY B 145 |
| Chain | Residue |
| B | TYR33 |
| B | HEM144 |
Functional Information from PROSITE/UniProt
| site_id | PS01213 |
| Number of Residues | 21 |
| Details | GLOBIN_FAM_2 Protozoan/cyanobacterial globins signature. FFaaalGGPepYtGAp....MkqvH |
| Chain | Residue | Details |
| A | PHE61-HIS81 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: proximal binding residue |
| Chain | Residue | Details |
| A | HIS81 | |
| B | HIS81 |
