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2YFI

Crystal Structure of Biphenyl dioxygenase variant RR41 (BPDO-RR41)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0018687molecular_functionbiphenyl 2,3-dioxygenase activity
A0051537molecular_function2 iron, 2 sulfur cluster binding
B0018687molecular_functionbiphenyl 2,3-dioxygenase activity
B0019380biological_process3-phenylpropionate catabolic process
C0005506molecular_functioniron ion binding
C0018687molecular_functionbiphenyl 2,3-dioxygenase activity
C0051537molecular_function2 iron, 2 sulfur cluster binding
D0018687molecular_functionbiphenyl 2,3-dioxygenase activity
D0019380biological_process3-phenylpropionate catabolic process
E0005506molecular_functioniron ion binding
E0018687molecular_functionbiphenyl 2,3-dioxygenase activity
E0051537molecular_function2 iron, 2 sulfur cluster binding
F0018687molecular_functionbiphenyl 2,3-dioxygenase activity
F0019380biological_process3-phenylpropionate catabolic process
G0005506molecular_functioniron ion binding
G0018687molecular_functionbiphenyl 2,3-dioxygenase activity
G0051537molecular_function2 iron, 2 sulfur cluster binding
H0018687molecular_functionbiphenyl 2,3-dioxygenase activity
H0019380biological_process3-phenylpropionate catabolic process
I0005506molecular_functioniron ion binding
I0018687molecular_functionbiphenyl 2,3-dioxygenase activity
I0051537molecular_function2 iron, 2 sulfur cluster binding
J0018687molecular_functionbiphenyl 2,3-dioxygenase activity
J0019380biological_process3-phenylpropionate catabolic process
K0005506molecular_functioniron ion binding
K0018687molecular_functionbiphenyl 2,3-dioxygenase activity
K0051537molecular_function2 iron, 2 sulfur cluster binding
L0018687molecular_functionbiphenyl 2,3-dioxygenase activity
L0019380biological_process3-phenylpropionate catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES A 900
ChainResidue
ACYS100
AHIS102
AARG103
ACYS120
AHIS123
ATRP125

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A 901
ChainResidue
AASP388
AHOH2125
AGLN226
AHIS233
AHIS239

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES C 900
ChainResidue
CCYS100
CHIS102
CARG103
CCYS120
CHIS123
CTRP125

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 C 901
ChainResidue
CGLN226
CHIS233
CHIS239
CASP388
CHOH2165

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES E 900
ChainResidue
ECYS100
EHIS102
EARG103
ECYS120
EHIS123
ETRP125

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 E 901
ChainResidue
EGLN226
EHIS233
EHIS239
EASP388
EHOH2091

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES G 900
ChainResidue
GCYS100
GHIS102
GARG103
GCYS120
GHIS123
GTRP125

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 G 901
ChainResidue
GGLN226
GHIS233
GHIS239
GASP388
GHOH2038

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES I 900
ChainResidue
ICYS100
IHIS102
IARG103
ICYS120
IHIS123
ITRP125

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 I 901
ChainResidue
IGLN226
IHIS233
IHIS239
IASP388
IHOH2030

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES K 900
ChainResidue
KCYS100
KHIS102
KARG103
KCYS120
KHIS123
KTRP125

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 K 901
ChainResidue
KGLN226
KHIS233
KHIS239
KASP388
KHOH2034

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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PDB entries from 2026-04-01

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