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1ULJ

Biphenyl dioxygenase (BphA1A2) in complex with the substrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0018687molecular_functionbiphenyl 2,3-dioxygenase activity
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0051536molecular_functioniron-sulfur cluster binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
B0005515molecular_functionprotein binding
B0016491molecular_functionoxidoreductase activity
B0018687molecular_functionbiphenyl 2,3-dioxygenase activity
B0019380biological_process3-phenylpropionate catabolic process
B0051213molecular_functiondioxygenase activity
C0004497molecular_functionmonooxygenase activity
C0005506molecular_functioniron ion binding
C0005515molecular_functionprotein binding
C0016491molecular_functionoxidoreductase activity
C0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C0018687molecular_functionbiphenyl 2,3-dioxygenase activity
C0046872molecular_functionmetal ion binding
C0051213molecular_functiondioxygenase activity
C0051536molecular_functioniron-sulfur cluster binding
C0051537molecular_function2 iron, 2 sulfur cluster binding
D0005515molecular_functionprotein binding
D0016491molecular_functionoxidoreductase activity
D0018687molecular_functionbiphenyl 2,3-dioxygenase activity
D0019380biological_process3-phenylpropionate catabolic process
D0051213molecular_functiondioxygenase activity
E0004497molecular_functionmonooxygenase activity
E0005506molecular_functioniron ion binding
E0005515molecular_functionprotein binding
E0016491molecular_functionoxidoreductase activity
E0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
E0018687molecular_functionbiphenyl 2,3-dioxygenase activity
E0046872molecular_functionmetal ion binding
E0051213molecular_functiondioxygenase activity
E0051536molecular_functioniron-sulfur cluster binding
E0051537molecular_function2 iron, 2 sulfur cluster binding
F0005515molecular_functionprotein binding
F0016491molecular_functionoxidoreductase activity
F0018687molecular_functionbiphenyl 2,3-dioxygenase activity
F0019380biological_process3-phenylpropionate catabolic process
F0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A 600
ChainResidue
AGLN217
AHIS224
AHIS230
AASP378
AHOH671

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 C 600
ChainResidue
CGLN217
CHIS224
CHIS230
CASP378

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 E 600
ChainResidue
EGLN217
EHIS224
EHIS230
EASP378

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES A 500
ChainResidue
ACYS98
AHIS100
AARG101
ACYS118
AHIS121
ATRP123

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES C 500
ChainResidue
CCYS98
CHIS100
CARG101
CCYS118
CHIS121
CTRP123

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES E 500
ChainResidue
ECYS98
EHIS100
EARG101
ECYS118
EHIS121
ETRP123

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BNL A 601
ChainResidue
AGLN217
AASP221
AMET222
AHIS224
AALA225
AILE278
AHIS313

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE BNL C 1001
ChainResidue
CGLN217
CASP221
CMET222
CHIS224
CALA225
CHIS230
CILE278
CHIS313

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BNL E 2001
ChainResidue
EGLN217
EPHE218
EASP221
EMET222
EALA225
EHIS230
EILE278
EHIS313
ELEU323

Functional Information from PROSITE/UniProt
site_idPS00570
Number of Residues24
DetailsRING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CrHRGmricradgGNaksftCsYH
ChainResidueDetails
ACYS98-HIS121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues327
DetailsDomain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues21
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15342255","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ULI","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"1ULJ","evidenceCode":"ECO:0000312"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues39
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15342255","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ndo
ChainResidueDetails
AHIS121
CASP221
CHIS224

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ndo
ChainResidueDetails
CHIS121
EASP221
EHIS224

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ndo
ChainResidueDetails
AASP221
AHIS224
EHIS121

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PDB entries from 2025-08-06

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