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 | 0019439 | biological_process | obsolete aromatic compound 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 | 0006725 | biological_process | obsolete cellular aromatic compound metabolic process |
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 | 0019439 | biological_process | obsolete aromatic compound 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 | 0006725 | biological_process | obsolete cellular aromatic compound metabolic process |
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 | 0019439 | biological_process | obsolete aromatic compound 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 | 0006725 | biological_process | obsolete cellular aromatic compound metabolic process |
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 |