5AEU
Crystal structure of II9 variant of Biphenyl dioxygenase from Burkholderia xenovorans LB400
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0018687 | molecular_function | biphenyl 2,3-dioxygenase activity |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0018687 | molecular_function | biphenyl 2,3-dioxygenase activity |
| B | 0019380 | biological_process | 3-phenylpropionate catabolic process |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0018687 | molecular_function | biphenyl 2,3-dioxygenase activity |
| C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| D | 0018687 | molecular_function | biphenyl 2,3-dioxygenase activity |
| D | 0019380 | biological_process | 3-phenylpropionate catabolic process |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0018687 | molecular_function | biphenyl 2,3-dioxygenase activity |
| E | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| F | 0018687 | molecular_function | biphenyl 2,3-dioxygenase activity |
| F | 0019380 | biological_process | 3-phenylpropionate catabolic process |
| G | 0005506 | molecular_function | iron ion binding |
| G | 0018687 | molecular_function | biphenyl 2,3-dioxygenase activity |
| G | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| H | 0018687 | molecular_function | biphenyl 2,3-dioxygenase activity |
| H | 0019380 | biological_process | 3-phenylpropionate catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FES A 500 |
| Chain | Residue |
| A | CYS100 |
| A | HIS102 |
| A | ARG103 |
| A | CYS120 |
| A | HIS123 |
| A | TRP125 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE2 A 501 |
| Chain | Residue |
| A | ASP388 |
| A | HOH2059 |
| A | HOH2063 |
| A | HOH2066 |
| A | GLN226 |
| A | HIS233 |
| A | HIS239 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES C 500 |
| Chain | Residue |
| C | CYS100 |
| C | HIS102 |
| C | ARG103 |
| C | CYS120 |
| C | HIS123 |
| C | GLY124 |
| C | TRP125 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE2 C 501 |
| Chain | Residue |
| C | GLN226 |
| C | HIS233 |
| C | HIS239 |
| C | ASP388 |
| C | HOH2020 |
| C | HOH2022 |
| C | HOH2025 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES E 500 |
| Chain | Residue |
| E | CYS100 |
| E | HIS102 |
| E | ARG103 |
| E | CYS120 |
| E | TYR122 |
| E | HIS123 |
| E | TRP125 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE2 E 501 |
| Chain | Residue |
| E | GLN226 |
| E | HIS233 |
| E | HIS239 |
| E | ASP388 |
| E | HOH2012 |
| E | HOH2013 |
| E | HOH2017 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FES G 500 |
| Chain | Residue |
| G | CYS100 |
| G | HIS102 |
| G | ARG103 |
| G | CYS120 |
| G | HIS123 |
| G | TRP125 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE2 G 501 |
| Chain | Residue |
| G | GLN226 |
| G | HIS233 |
| G | HIS239 |
| G | ASP388 |
| G | HOH2005 |
| G | HOH2013 |
Functional Information from PROSITE/UniProt
| site_id | PS00570 |
| Number of Residues | 24 |
| Details | RING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CrHRGmricrsdaGNakaftCsYH |
| Chain | Residue | Details |
| A | CYS100-HIS123 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
