6EXF
Crystal structure of the complex Fe(II)/alpha-ketoglutarate dependent dioxygenase KDO5 with Fe(II)/Lysine
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 | 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 | 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 | 6 |
Details | binding site for residue FE A 401 |
Chain | Residue |
A | HIS176 |
A | GLU178 |
A | HIS312 |
A | LYS403 |
A | HOH672 |
A | HOH684 |
site_id | AC2 |
Number of Residues | 13 |
Details | binding site for residue LYS A 402 |
Chain | Residue |
A | TYR193 |
A | SER202 |
A | THR203 |
A | GLY313 |
A | ARG314 |
A | ARG334 |
A | MET336 |
A | HOH512 |
A | HOH672 |
A | HOH684 |
A | VAL154 |
A | THR165 |
A | GLY166 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue LYS A 403 |
Chain | Residue |
A | GLN144 |
A | ARG145 |
A | GLY166 |
A | SER167 |
A | ARG338 |
A | FE401 |
A | HOH646 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue FE B 401 |
Chain | Residue |
B | HIS176 |
B | GLU178 |
B | HIS312 |
B | LYS402 |
B | HOH634 |
B | HOH640 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue LYS B 402 |
Chain | Residue |
B | GLN144 |
B | HIS176 |
B | GLU178 |
B | ASP230 |
B | ASP260 |
B | ARG314 |
B | ARG338 |
B | FE401 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue FE C 401 |
Chain | Residue |
C | HIS176 |
C | GLU178 |
C | HIS312 |
C | HOH662 |
site_id | AC7 |
Number of Residues | 12 |
Details | binding site for residue LYS C 402 |
Chain | Residue |
C | GLN144 |
C | ARG145 |
C | VAL154 |
C | THR165 |
C | GLY166 |
C | SER167 |
C | HIS176 |
C | ASN232 |
C | ARG338 |
C | HOH524 |
C | HOH578 |
C | HOH619 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue GOL C 403 |
Chain | Residue |
C | GLN102 |
C | ASP103 |
C | GLY106 |
C | PRO107 |
C | ARG195 |
C | GLU332 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue FE D 401 |
Chain | Residue |
D | HIS176 |
D | GLU178 |
D | HIS312 |
D | LYS402 |
D | HOH673 |
site_id | AD1 |
Number of Residues | 10 |
Details | binding site for residue LYS D 402 |
Chain | Residue |
D | GLN164 |
D | THR165 |
D | GLY166 |
D | HIS176 |
D | GLU178 |
D | ASP230 |
D | ASP260 |
D | ARG338 |
D | FE401 |
D | HOH616 |
site_id | AD2 |
Number of Residues | 1 |
Details | binding site for residue GOL D 403 |
Chain | Residue |
D | PHE49 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9Z4Z5 |
Chain | Residue | Details |
A | HIS176 | |
D | HIS176 | |
D | GLU178 | |
D | HIS312 | |
A | GLU178 | |
A | HIS312 | |
B | HIS176 | |
B | GLU178 | |
B | HIS312 | |
C | HIS176 | |
C | GLU178 | |
C | HIS312 |