2GBX
Crystal Structure of Biphenyl 2,3-Dioxygenase from Sphingomonas yanoikuyae B1 Bound to Biphenyl
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 | 0046872 | molecular_function | metal ion binding |
| 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 | 0046872 | molecular_function | metal ion binding |
| 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 | 0046872 | molecular_function | metal ion binding |
| F | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE A 456 |
| Chain | Residue |
| A | HIS207 |
| A | HIS212 |
| A | ASP360 |
| A | HOH463 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE C 456 |
| Chain | Residue |
| C | HIS207 |
| C | HIS212 |
| C | ASP360 |
| C | HOH460 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE E 456 |
| Chain | Residue |
| E | HIS212 |
| E | ASP360 |
| E | HOH494 |
| E | HIS207 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 460 |
| Chain | Residue |
| B | HIS19 |
| B | MET39 |
| B | HOH491 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 462 |
| Chain | Residue |
| D | HIS136 |
| D | HOH470 |
| D | HOH471 |
| D | HOH489 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN F 463 |
| Chain | Residue |
| F | HIS136 |
| F | HOH468 |
| F | HOH469 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 464 |
| Chain | Residue |
| B | HIS136 |
| B | HOH469 |
| B | HOH470 |
| B | HOH476 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN D 465 |
| Chain | Residue |
| D | HIS19 |
| D | HOH488 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN F 466 |
| Chain | Residue |
| F | HIS45 |
| F | HOH470 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ZN F 467 |
| Chain | Residue |
| F | HIS19 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 468 |
| Chain | Residue |
| B | HIS45 |
| B | ARG155 |
| B | HOH495 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN D 469 |
| Chain | Residue |
| D | HIS45 |
| D | ARG155 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FES A 455 |
| Chain | Residue |
| A | CYS80 |
| A | HIS82 |
| A | ARG83 |
| A | ASN85 |
| A | CYS100 |
| A | TYR102 |
| A | HIS103 |
| A | TRP105 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BNL A 457 |
| Chain | Residue |
| A | ASN200 |
| A | ASP204 |
| A | VAL208 |
| A | LEU223 |
| A | LEU260 |
| A | HIS293 |
| A | ASN295 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES C 455 |
| Chain | Residue |
| C | CYS80 |
| C | HIS82 |
| C | ARG83 |
| C | CYS100 |
| C | TYR102 |
| C | HIS103 |
| C | TRP105 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BNL C 458 |
| Chain | Residue |
| C | ASN200 |
| C | ASP204 |
| C | VAL208 |
| C | LEU223 |
| C | LEU260 |
| C | HIS293 |
| C | ASN295 |
| site_id | BC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FES E 455 |
| Chain | Residue |
| E | CYS80 |
| E | HIS82 |
| E | ARG83 |
| E | ASN85 |
| E | CYS100 |
| E | TYR102 |
| E | HIS103 |
| E | TRP105 |
| site_id | BC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BNL E 459 |
| Chain | Residue |
| E | ASN200 |
| E | ASP204 |
| E | VAL208 |
| E | LEU223 |
| E | LEU260 |
| E | HIS293 |
| E | ASN295 |
| E | LEU305 |
Functional Information from PROSITE/UniProt
| site_id | PS00570 |
| Number of Residues | 24 |
| Details | RING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CsHRGnqichadsGNakafvCnYH |
| 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 |
