4Y0E
X-ray Crystal Structure of a putative dioxygenase from Mycobacterium abscessus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051213 | molecular_function | dioxygenase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051213 | molecular_function | dioxygenase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051213 | molecular_function | dioxygenase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051213 | molecular_function | dioxygenase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0051213 | molecular_function | dioxygenase activity |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0051213 | molecular_function | dioxygenase activity |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue FE A 401 |
| Chain | Residue |
| A | HIS104 |
| A | ASP106 |
| A | HIS262 |
| A | ARG277 |
| A | HOH670 |
| A | HOH671 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue MPD A 402 |
| Chain | Residue |
| A | HIS200 |
| A | GLU202 |
| A | ASP256 |
| A | HOH688 |
| A | ARG47 |
| A | ALA51 |
| A | LYS115 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue EPE A 403 |
| Chain | Residue |
| A | HIS83 |
| A | ALA100 |
| A | HIS104 |
| A | ASP106 |
| A | VAL107 |
| A | TYR162 |
| A | PHE185 |
| A | GLN212 |
| A | PHE213 |
| A | ARG277 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue FE B 401 |
| Chain | Residue |
| B | HIS104 |
| B | ASP106 |
| B | HIS262 |
| B | HOH567 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue MPD B 402 |
| Chain | Residue |
| B | ARG47 |
| B | ALA51 |
| B | LYS115 |
| B | HIS200 |
| B | GLU202 |
| B | ASP256 |
| B | LEU312 |
| B | HOH766 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue EPE B 403 |
| Chain | Residue |
| B | HIS83 |
| B | ALA100 |
| B | HIS104 |
| B | ASP106 |
| B | VAL107 |
| B | PHE185 |
| B | GLN212 |
| B | PHE213 |
| B | ARG277 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue FE C 401 |
| Chain | Residue |
| C | HIS104 |
| C | ASP106 |
| C | HIS262 |
| C | ARG277 |
| C | HOH794 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue MPD C 402 |
| Chain | Residue |
| C | ARG47 |
| C | LYS115 |
| C | HIS200 |
| C | GLU202 |
| C | ASP256 |
| C | HOH602 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | binding site for residue EPE C 403 |
| Chain | Residue |
| C | HIS83 |
| C | ALA100 |
| C | HIS104 |
| C | ASP106 |
| C | VAL107 |
| C | TYR162 |
| C | PHE185 |
| C | GLN212 |
| C | PHE213 |
| C | ARG277 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue FE D 401 |
| Chain | Residue |
| D | HIS104 |
| D | ASP106 |
| D | HIS262 |
| D | HOH559 |
| D | HOH663 |
| site_id | AD2 |
| Number of Residues | 10 |
| Details | binding site for residue MPD D 402 |
| Chain | Residue |
| D | ARG47 |
| D | LEU50 |
| D | ALA51 |
| D | LYS115 |
| D | HIS200 |
| D | GLU202 |
| D | ASP256 |
| D | LEU312 |
| D | HOH561 |
| D | HOH680 |
| site_id | AD3 |
| Number of Residues | 10 |
| Details | binding site for residue EPE D 403 |
| Chain | Residue |
| D | HIS83 |
| D | ALA100 |
| D | ASN101 |
| D | HIS104 |
| D | ASP106 |
| D | VAL107 |
| D | PHE185 |
| D | GLN212 |
| D | PHE213 |
| D | ARG277 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue FE E 401 |
| Chain | Residue |
| E | HIS104 |
| E | ASP106 |
| E | HIS262 |
| E | ARG277 |
| E | HOH636 |
| E | HOH670 |
| E | HOH706 |
| site_id | AD5 |
| Number of Residues | 8 |
| Details | binding site for residue MPD E 402 |
| Chain | Residue |
| E | ALA51 |
| E | LYS115 |
| E | HIS200 |
| E | GLU202 |
| E | ASP256 |
| E | HOH572 |
| E | ARG47 |
| E | LEU50 |
| site_id | AD6 |
| Number of Residues | 9 |
| Details | binding site for residue EPE E 403 |
| Chain | Residue |
| E | HIS83 |
| E | ASN101 |
| E | HIS104 |
| E | ASP106 |
| E | VAL107 |
| E | GLN212 |
| E | PHE213 |
| E | ARG277 |
| E | HOH670 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue FE F 401 |
| Chain | Residue |
| F | HIS104 |
| F | ASP106 |
| F | HIS262 |
| F | ARG277 |
| F | HOH560 |
| site_id | AD8 |
| Number of Residues | 7 |
| Details | binding site for residue MPD F 402 |
| Chain | Residue |
| F | ARG47 |
| F | ALA51 |
| F | LYS115 |
| F | ALA116 |
| F | GLU202 |
| F | ASP256 |
| F | HOH602 |
| site_id | AD9 |
| Number of Residues | 10 |
| Details | binding site for residue EPE F 403 |
| Chain | Residue |
| F | HIS83 |
| F | ALA100 |
| F | HIS104 |
| F | ASP106 |
| F | VAL107 |
| F | TYR162 |
| F | PHE185 |
| F | GLN212 |
| F | PHE213 |
| F | ARG277 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue FE G 401 |
| Chain | Residue |
| G | HIS104 |
| G | ASP106 |
| G | HIS262 |
| G | ARG277 |
| G | HOH600 |
| site_id | AE2 |
| Number of Residues | 8 |
| Details | binding site for residue MRD G 402 |
| Chain | Residue |
| G | ARG47 |
| G | LEU50 |
| G | ALA51 |
| G | LYS115 |
| G | GLU202 |
| G | ASP256 |
| G | LEU312 |
| G | HOH567 |
| site_id | AE3 |
| Number of Residues | 11 |
| Details | binding site for residue EPE G 403 |
| Chain | Residue |
| G | HIS83 |
| G | ALA100 |
| G | ASN101 |
| G | HIS104 |
| G | ASP106 |
| G | VAL107 |
| G | TYR162 |
| G | PHE185 |
| G | GLN212 |
| G | PHE213 |
| G | ARG277 |
| site_id | AE4 |
| Number of Residues | 6 |
| Details | binding site for residue FE H 401 |
| Chain | Residue |
| H | HIS104 |
| H | ASP106 |
| H | HIS262 |
| H | ARG277 |
| H | HOH546 |
| H | HOH699 |
| site_id | AE5 |
| Number of Residues | 8 |
| Details | binding site for residue MRD H 402 |
| Chain | Residue |
| H | ARG47 |
| H | ALA51 |
| H | LYS115 |
| H | HIS200 |
| H | GLU202 |
| H | ASP256 |
| H | LEU312 |
| H | HOH614 |
| site_id | AE6 |
| Number of Residues | 10 |
| Details | binding site for residue EPE H 403 |
| Chain | Residue |
| H | HIS83 |
| H | ALA100 |
| H | HIS104 |
| H | ASP106 |
| H | VAL107 |
| H | TYR162 |
| H | PHE185 |
| H | GLN212 |
| H | PHE213 |
| H | ARG277 |
