6F2B
Crystal structure of the complex Fe(II)/alpha-ketoglutarate dependent dioxygenase KDO1 with Fe(II)/alpha-ketoglutarate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005506 | molecular_function | iron ion binding |
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 |
A | 0055114 | biological_process | obsolete oxidation-reduction process |
B | 0005506 | molecular_function | iron ion binding |
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 |
B | 0055114 | biological_process | obsolete oxidation-reduction process |
C | 0005506 | molecular_function | iron ion binding |
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 |
C | 0055114 | biological_process | obsolete oxidation-reduction process |
D | 0005506 | molecular_function | iron ion binding |
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 |
D | 0055114 | biological_process | obsolete oxidation-reduction process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue FE2 A 401 |
Chain | Residue |
A | HIS178 |
A | GLU180 |
A | HIS314 |
A | AKG402 |
A | HOH536 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue AKG A 402 |
Chain | Residue |
A | LEU193 |
A | THR204 |
A | HIS314 |
A | ARG316 |
A | ARG328 |
A | ARG332 |
A | FE2401 |
A | HOH533 |
A | MET156 |
A | LEU175 |
A | HIS178 |
A | GLU180 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue FE2 B 401 |
Chain | Residue |
B | HIS178 |
B | GLU180 |
B | HIS314 |
B | AKG402 |
B | HOH654 |
site_id | AC4 |
Number of Residues | 12 |
Details | binding site for residue AKG B 402 |
Chain | Residue |
B | LEU175 |
B | GLU180 |
B | VAL191 |
B | LEU193 |
B | THR204 |
B | HIS314 |
B | ARG316 |
B | ARG328 |
B | LEU330 |
B | ARG332 |
B | FE2401 |
B | HOH543 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue FE2 C 401 |
Chain | Residue |
C | HIS178 |
C | GLU180 |
C | HIS314 |
C | AKG402 |
C | HOH600 |
site_id | AC6 |
Number of Residues | 12 |
Details | binding site for residue AKG C 402 |
Chain | Residue |
C | MET156 |
C | LEU175 |
C | HIS178 |
C | GLU180 |
C | LEU193 |
C | THR204 |
C | HIS314 |
C | ARG316 |
C | ARG328 |
C | ARG332 |
C | FE2401 |
C | HOH556 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue FE2 D 401 |
Chain | Residue |
D | HIS178 |
D | GLU180 |
D | HIS314 |
D | AKG402 |
D | HOH693 |
site_id | AC8 |
Number of Residues | 12 |
Details | binding site for residue AKG D 402 |
Chain | Residue |
D | LEU175 |
D | HIS178 |
D | GLU180 |
D | LEU193 |
D | THR204 |
D | HIS314 |
D | ARG316 |
D | ARG328 |
D | LEU330 |
D | ARG332 |
D | FE2401 |
D | HOH517 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9Z4Z5 |
Chain | Residue | Details |
A | HIS178 | |
C | GLU180 | |
C | HIS314 | |
C | ARG328 | |
D | HIS178 | |
D | GLU180 | |
D | HIS314 | |
D | ARG328 | |
A | GLU180 | |
A | HIS314 | |
A | ARG328 | |
B | HIS178 | |
B | GLU180 | |
B | HIS314 | |
B | ARG328 | |
C | HIS178 |