2CKF
Crystal Structure of the Terminal Component of the PAH-hydroxylating Dioxygenase from Sphingomonas sp CHY-1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019380 | biological_process | 3-phenylpropionate catabolic process |
| B | 0051213 | molecular_function | dioxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051213 | molecular_function | dioxygenase activity |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0019380 | biological_process | 3-phenylpropionate catabolic process |
| D | 0051213 | molecular_function | dioxygenase activity |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051213 | molecular_function | dioxygenase activity |
| E | 0051536 | molecular_function | iron-sulfur cluster binding |
| E | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0019380 | biological_process | 3-phenylpropionate catabolic process |
| F | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE A 501 |
| Chain | Residue |
| A | HIS207 |
| A | HIS212 |
| A | ASP360 |
| A | HOH2204 |
| A | HOH2281 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE C 501 |
| Chain | Residue |
| C | HIS207 |
| C | HIS212 |
| C | ASP360 |
| C | HOH2106 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE E 501 |
| Chain | Residue |
| E | HIS207 |
| E | HIS212 |
| E | ASP360 |
| E | HOH2087 |
| E | HOH2088 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FES A 500 |
| Chain | Residue |
| A | CYS80 |
| A | HIS82 |
| A | ARG83 |
| A | CYS100 |
| A | HIS103 |
| A | TRP105 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FES C 500 |
| Chain | Residue |
| C | CYS80 |
| C | HIS82 |
| C | ARG83 |
| C | CYS100 |
| C | TYR102 |
| C | HIS103 |
| C | GLY104 |
| C | TRP105 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES E 500 |
| Chain | Residue |
| E | CYS80 |
| E | HIS82 |
| E | ARG83 |
| E | CYS100 |
| E | TYR102 |
| E | HIS103 |
| E | TRP105 |
Functional Information from PROSITE/UniProt
| site_id | PS00570 |
| Number of Residues | 24 |
| Details | RING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CtHRGnqichadsGNakafvCnYH |
| Chain | Residue | Details |
| A | CYS80-HIS103 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ndo |
| Chain | Residue | Details |
| A | HIS103 | |
| E | HIS207 | |
| E | ASP204 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ndo |
| Chain | Residue | Details |
| A | ASP204 | |
| A | HIS207 | |
| C | HIS103 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ndo |
| Chain | Residue | Details |
| C | ASP204 | |
| C | HIS207 | |
| E | HIS103 |
