1S56
Crystal Structure of "Truncated" Hemoglobin N (HbN) from Mycobacterium tuberculosis, Soaked with Xe Atoms
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 | 4 |
Details | BINDING SITE FOR RESIDUE CYN A 145 |
Chain | Residue |
A | TYR33 |
A | PHE46 |
A | GLN58 |
A | HEC144 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CYN B 245 |
Chain | Residue |
B | TYR33 |
B | HEM144 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 B 301 |
Chain | Residue |
B | TYR16 |
B | GLY21 |
B | HIS22 |
B | GLY2 |
B | LEU3 |
B | ARG6 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K A 401 |
Chain | Residue |
A | GLN79 |
A | VAL80 |
A | GLN82 |
B | GLY83 |
site_id | AC5 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE HEC A 144 |
Chain | Residue |
A | PHE45 |
A | PHE46 |
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 | ILE119 |
A | VAL126 |
A | CYN145 |
A | XE203 |
site_id | AC6 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE HEM B 144 |
Chain | Residue |
B | PHE45 |
B | THR49 |
B | ARG53 |
B | LEU54 |
B | LYS57 |
B | GLN58 |
B | PHE61 |
B | TYR72 |
B | GLY74 |
B | ALA75 |
B | MET77 |
B | VAL80 |
B | HIS81 |
B | ARG84 |
B | ILE86 |
B | PHE91 |
B | VAL94 |
B | VAL126 |
B | XE204 |
B | CYN245 |
B | HOH326 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE XE A 203 |
Chain | Residue |
A | PHE62 |
A | HEC144 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE XE B 204 |
Chain | Residue |
B | PHE32 |
B | PHE62 |
B | VAL94 |
B | HEM144 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE XE B 205 |
Chain | Residue |
B | ILE119 |
B | ALA120 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE XE B 206 |
Chain | Residue |
B | LEU3 |
B | ASP17 |
B | LEU116 |
B | ALA120 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE XE A 207 |
Chain | Residue |
A | PHE32 |
A | PHE62 |
A | LEU98 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE XE A 208 |
Chain | Residue |
A | LEU3 |
A | ALA120 |
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 |