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 | 0009056 | biological_process | catabolic process |
A | 0044237 | biological_process | cellular metabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0051213 | molecular_function | dioxygenase activity |
A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
B | 0019380 | biological_process | 3-phenylpropionate catabolic process |
B | 0051213 | molecular_function | dioxygenase activity |
C | 0005506 | molecular_function | iron ion binding |
C | 0009056 | biological_process | catabolic process |
C | 0044237 | biological_process | cellular metabolic process |
C | 0046872 | molecular_function | metal ion binding |
C | 0051213 | molecular_function | dioxygenase activity |
C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
D | 0019380 | biological_process | 3-phenylpropionate catabolic process |
D | 0051213 | molecular_function | dioxygenase activity |
E | 0005506 | molecular_function | iron ion binding |
E | 0009056 | biological_process | catabolic process |
E | 0044237 | biological_process | cellular metabolic process |
E | 0046872 | molecular_function | metal ion binding |
E | 0051213 | molecular_function | dioxygenase activity |
E | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
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 |