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3GZY

Crystal Structure of the Biphenyl Dioxygenase from Comamonas testosteroni Sp. Strain B-356

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0016491molecular_functionoxidoreductase activity
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
B0016491molecular_functionoxidoreductase activity
B0018687molecular_functionbiphenyl 2,3-dioxygenase activity
B0019380biological_process3-phenylpropionate catabolic process
B0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A 701
ChainResidue
AGLN226
AHIS233
AHIS239
AASP386
AHOH514

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES A 700
ChainResidue
AHIS123
ATRP125
ACYS100
AHIS102
AARG103
ACYS120

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MES B 702
ChainResidue
AASN279
AHOH641
AHOH797
AHOH825
BARG118
BMET120
BASP121
BHOH271

Functional Information from PROSITE/UniProt
site_idPS00570
Number of Residues24
DetailsRING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CrHRGmrivrsdgGNakaftCtYH
ChainResidueDetails
ACYS100-HIS123

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues116
DetailsDomain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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