7VJU
Crystal Structure of terephthalate dioxygenase from Comamonas testosteroni KF1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005506 | molecular_function | iron ion binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0044237 | biological_process | cellular metabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
B | 0051213 | molecular_function | dioxygenase activity |
C | 0005506 | molecular_function | iron ion binding |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0044237 | biological_process | cellular metabolic process |
C | 0046872 | molecular_function | metal ion binding |
C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
D | 0051213 | molecular_function | dioxygenase activity |
E | 0005506 | molecular_function | iron ion binding |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0044237 | biological_process | cellular metabolic process |
E | 0046872 | molecular_function | metal ion binding |
E | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
F | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PROSITE/UniProt
site_id | PS00570 |
Number of Residues | 24 |
Details | RING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CaHRGalialeksGRtdsfqCvYH |
Chain | Residue | Details |
A | CYS82-HIS105 |