1ULJ
Biphenyl dioxygenase (BphA1A2) in complex with the substrate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005506 | molecular_function | iron ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0018687 | molecular_function | biphenyl 2,3-dioxygenase activity |
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 | 0005515 | molecular_function | protein binding |
B | 0006725 | biological_process | obsolete cellular aromatic compound metabolic process |
B | 0018687 | molecular_function | biphenyl 2,3-dioxygenase activity |
B | 0019380 | biological_process | 3-phenylpropionate catabolic process |
B | 0019439 | biological_process | obsolete aromatic compound catabolic process |
B | 0051213 | molecular_function | dioxygenase activity |
C | 0005506 | molecular_function | iron ion binding |
C | 0005515 | molecular_function | protein binding |
C | 0018687 | molecular_function | biphenyl 2,3-dioxygenase activity |
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 | 0005515 | molecular_function | protein binding |
D | 0006725 | biological_process | obsolete cellular aromatic compound metabolic process |
D | 0018687 | molecular_function | biphenyl 2,3-dioxygenase activity |
D | 0019380 | biological_process | 3-phenylpropionate catabolic process |
D | 0019439 | biological_process | obsolete aromatic compound catabolic process |
D | 0051213 | molecular_function | dioxygenase activity |
E | 0005506 | molecular_function | iron ion binding |
E | 0005515 | molecular_function | protein binding |
E | 0018687 | molecular_function | biphenyl 2,3-dioxygenase activity |
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 | 0005515 | molecular_function | protein binding |
F | 0006725 | biological_process | obsolete cellular aromatic compound metabolic process |
F | 0018687 | molecular_function | biphenyl 2,3-dioxygenase activity |
F | 0019380 | biological_process | 3-phenylpropionate catabolic process |
F | 0019439 | biological_process | obsolete aromatic compound 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 FE2 A 600 |
Chain | Residue |
A | GLN217 |
A | HIS224 |
A | HIS230 |
A | ASP378 |
A | HOH671 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE2 C 600 |
Chain | Residue |
C | GLN217 |
C | HIS224 |
C | HIS230 |
C | ASP378 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE2 E 600 |
Chain | Residue |
E | GLN217 |
E | HIS224 |
E | HIS230 |
E | ASP378 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FES A 500 |
Chain | Residue |
A | CYS98 |
A | HIS100 |
A | ARG101 |
A | CYS118 |
A | HIS121 |
A | TRP123 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FES C 500 |
Chain | Residue |
C | CYS98 |
C | HIS100 |
C | ARG101 |
C | CYS118 |
C | HIS121 |
C | TRP123 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FES E 500 |
Chain | Residue |
E | CYS98 |
E | HIS100 |
E | ARG101 |
E | CYS118 |
E | HIS121 |
E | TRP123 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE BNL A 601 |
Chain | Residue |
A | GLN217 |
A | ASP221 |
A | MET222 |
A | HIS224 |
A | ALA225 |
A | ILE278 |
A | HIS313 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BNL C 1001 |
Chain | Residue |
C | GLN217 |
C | ASP221 |
C | MET222 |
C | HIS224 |
C | ALA225 |
C | HIS230 |
C | ILE278 |
C | HIS313 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE BNL E 2001 |
Chain | Residue |
E | GLN217 |
E | PHE218 |
E | ASP221 |
E | MET222 |
E | ALA225 |
E | HIS230 |
E | ILE278 |
E | HIS313 |
E | LEU323 |
Functional Information from PROSITE/UniProt
site_id | PS00570 |
Number of Residues | 24 |
Details | RING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CrHRGmricradgGNaksftCsYH |
Chain | Residue | Details |
A | CYS98-HIS121 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 21 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15342255, ECO:0000312|PDB:1ULI, ECO:0000312|PDB:1ULJ |
Chain | Residue | Details |
A | CYS98 | |
C | CYS118 | |
C | HIS121 | |
C | HIS224 | |
C | HIS230 | |
C | ASP378 | |
E | CYS98 | |
E | HIS100 | |
E | CYS118 | |
E | HIS121 | |
E | HIS224 | |
A | HIS100 | |
E | HIS230 | |
E | ASP378 | |
A | CYS118 | |
A | HIS121 | |
A | HIS224 | |
A | HIS230 | |
A | ASP378 | |
C | CYS98 | |
C | HIS100 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15342255 |
Chain | Residue | Details |
A | GLN217 | |
C | GLN217 | |
E | GLN217 |