Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2YFI

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0016491	molecular_function	oxidoreductase activity
A	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
A	0046872	molecular_function	metal ion binding
A	0051213	molecular_function	dioxygenase activity
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0016491	molecular_function	oxidoreductase activity
B	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
B	0019380	biological_process	3-phenylpropionate catabolic process
B	0051213	molecular_function	dioxygenase activity
C	0005506	molecular_function	iron ion binding
C	0016491	molecular_function	oxidoreductase activity
C	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
C	0046872	molecular_function	metal ion binding
C	0051213	molecular_function	dioxygenase activity
C	0051536	molecular_function	iron-sulfur cluster binding
C	0051537	molecular_function	2 iron, 2 sulfur cluster binding
D	0016491	molecular_function	oxidoreductase activity
D	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
D	0019380	biological_process	3-phenylpropionate catabolic process
D	0051213	molecular_function	dioxygenase activity
E	0005506	molecular_function	iron ion binding
E	0016491	molecular_function	oxidoreductase activity
E	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
E	0046872	molecular_function	metal ion binding
E	0051213	molecular_function	dioxygenase activity
E	0051536	molecular_function	iron-sulfur cluster binding
E	0051537	molecular_function	2 iron, 2 sulfur cluster binding
F	0016491	molecular_function	oxidoreductase activity
F	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
F	0019380	biological_process	3-phenylpropionate catabolic process
F	0051213	molecular_function	dioxygenase activity
G	0005506	molecular_function	iron ion binding
G	0016491	molecular_function	oxidoreductase activity
G	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
G	0046872	molecular_function	metal ion binding
G	0051213	molecular_function	dioxygenase activity
G	0051536	molecular_function	iron-sulfur cluster binding
G	0051537	molecular_function	2 iron, 2 sulfur cluster binding
H	0016491	molecular_function	oxidoreductase activity
H	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
H	0019380	biological_process	3-phenylpropionate catabolic process
H	0051213	molecular_function	dioxygenase activity
I	0005506	molecular_function	iron ion binding
I	0016491	molecular_function	oxidoreductase activity
I	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
I	0046872	molecular_function	metal ion binding
I	0051213	molecular_function	dioxygenase activity
I	0051536	molecular_function	iron-sulfur cluster binding
I	0051537	molecular_function	2 iron, 2 sulfur cluster binding
J	0016491	molecular_function	oxidoreductase activity
J	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
J	0019380	biological_process	3-phenylpropionate catabolic process
J	0051213	molecular_function	dioxygenase activity
K	0005506	molecular_function	iron ion binding
K	0016491	molecular_function	oxidoreductase activity
K	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
K	0046872	molecular_function	metal ion binding
K	0051213	molecular_function	dioxygenase activity
K	0051536	molecular_function	iron-sulfur cluster binding
K	0051537	molecular_function	2 iron, 2 sulfur cluster binding
L	0016491	molecular_function	oxidoreductase activity
L	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
L	0019380	biological_process	3-phenylpropionate catabolic process
L	0051213	molecular_function	dioxygenase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES A 900

Chain	Residue
A	CYS100
A	HIS102
A	ARG103
A	CYS120
A	HIS123
A	TRP125

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 A 901

Chain	Residue
A	ASP388
A	HOH2125
A	GLN226
A	HIS233
A	HIS239

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES C 900

Chain	Residue
C	CYS100
C	HIS102
C	ARG103
C	CYS120
C	HIS123
C	TRP125

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 C 901

Chain	Residue
C	GLN226
C	HIS233
C	HIS239
C	ASP388
C	HOH2165

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES E 900

Chain	Residue
E	CYS100
E	HIS102
E	ARG103
E	CYS120
E	HIS123
E	TRP125

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 E 901

Chain	Residue
E	GLN226
E	HIS233
E	HIS239
E	ASP388
E	HOH2091

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES G 900

Chain	Residue
G	CYS100
G	HIS102
G	ARG103
G	CYS120
G	HIS123
G	TRP125

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 G 901

Chain	Residue
G	GLN226
G	HIS233
G	HIS239
G	ASP388
G	HOH2038

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES I 900

Chain	Residue
I	CYS100
I	HIS102
I	ARG103
I	CYS120
I	HIS123
I	TRP125

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 I 901

Chain	Residue
I	GLN226
I	HIS233
I	HIS239
I	ASP388
I	HOH2030

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES K 900

Chain	Residue
K	CYS100
K	HIS102
K	ARG103
K	CYS120
K	HIS123
K	TRP125

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 K 901

Chain	Residue
K	GLN226
K	HIS233
K	HIS239
K	ASP388
K	HOH2034

Functional Information from PROSITE/UniProt

site_id	PS00570
Number of Residues	24
Details	RING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CrHRGmricrsdaGNakaftCsYH

Chain	Residue	Details
A	CYS100-HIS123

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)