Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2XSO

CRYSTAL STRUCTURE OF P4 VARIANT OF BIPHENYL DIOXYGENASE FROM BURKHOLDERIA XENOVORANS LB400

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
B	0019380	biological_process	3-phenylpropionate catabolic process
C	0005506	molecular_function	iron ion binding
C	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
C	0051537	molecular_function	2 iron, 2 sulfur cluster binding
D	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
D	0019380	biological_process	3-phenylpropionate catabolic process
E	0005506	molecular_function	iron ion binding
E	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
E	0051537	molecular_function	2 iron, 2 sulfur cluster binding
F	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
F	0019380	biological_process	3-phenylpropionate catabolic process
G	0005506	molecular_function	iron ion binding
G	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
G	0051537	molecular_function	2 iron, 2 sulfur cluster binding
H	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
H	0019380	biological_process	3-phenylpropionate catabolic process
I	0005506	molecular_function	iron ion binding
I	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
I	0051537	molecular_function	2 iron, 2 sulfur cluster binding
J	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
J	0019380	biological_process	3-phenylpropionate catabolic process
K	0005506	molecular_function	iron ion binding
K	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
K	0051537	molecular_function	2 iron, 2 sulfur cluster binding
L	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
L	0019380	biological_process	3-phenylpropionate catabolic process
M	0005506	molecular_function	iron ion binding
M	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
M	0051537	molecular_function	2 iron, 2 sulfur cluster binding
N	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
N	0019380	biological_process	3-phenylpropionate catabolic process
O	0005506	molecular_function	iron ion binding
O	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
O	0051537	molecular_function	2 iron, 2 sulfur cluster binding
P	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
P	0019380	biological_process	3-phenylpropionate catabolic process
Q	0005506	molecular_function	iron ion binding
Q	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
Q	0051537	molecular_function	2 iron, 2 sulfur cluster binding
R	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
R	0019380	biological_process	3-phenylpropionate catabolic process
S	0005506	molecular_function	iron ion binding
S	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
S	0051537	molecular_function	2 iron, 2 sulfur cluster binding
T	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
T	0019380	biological_process	3-phenylpropionate catabolic process
U	0005506	molecular_function	iron ion binding
U	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
U	0051537	molecular_function	2 iron, 2 sulfur cluster binding
V	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
V	0019380	biological_process	3-phenylpropionate catabolic process
W	0005506	molecular_function	iron ion binding
W	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
W	0051537	molecular_function	2 iron, 2 sulfur cluster binding
X	0018687	molecular_function	biphenyl 2,3-dioxygenase activity
X	0019380	biological_process	3-phenylpropionate catabolic process

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	HOH2097
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	HOH2069

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	HOH2119

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES G 900

Chain	Residue
G	CYS100
G	HIS102
G	ARG103
G	MET105
G	CYS120
G	TYR122
G	HIS123
G	TRP125

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 G 901

Chain	Residue
G	HIS233
G	HIS239
G	ASP388
G	HOH2154

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	HOH2055

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FES K 900

Chain	Residue
K	CYS100
K	HIS102
K	ARG103
K	MET105
K	CYS120
K	HIS123
K	TRP125
K	HOH2024
K	HOH2026

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 K 901

Chain	Residue
K	HIS233
K	HIS239
K	ASP388
K	HOH2060

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES M 900

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

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 M 901

Chain	Residue
M	GLN226
M	HIS233
M	HIS239
M	ASP388
M	HOH2081

site_id	BC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES O 900

Chain	Residue
O	CYS100
O	HIS102
O	ARG103
O	CYS120
O	HIS123
O	TRP125
O	HOH2035
O	HOH2036

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FE2 O 901

Chain	Residue
O	HIS233
O	HIS239
O	ASP388

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES Q 900

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

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 Q 901

Chain	Residue
Q	HIS239
Q	ASP388
Q	GLN226
Q	HIS233

site_id	CC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FES S 900

Chain	Residue
S	CYS100
S	HIS102
S	ARG103
S	CYS120
S	HIS123
S	TRP125
S	HOH2021
S	HOH2028
S	HOH2029

site_id	CC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FE2 S 901

Chain	Residue
S	HIS233
S	HIS239
S	ASP388

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES U 900

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

site_id	CC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE FE2 U 901

Chain	Residue
U	HIS239
U	ASP388

site_id	CC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES W 900

Chain	Residue
W	CYS100
W	HIS102
W	ARG103
W	CYS120
W	TYR122
W	HIS123
W	HOH2025

site_id	CC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 W 901

Chain	Residue
W	GLN226
W	HIS233
W	HIS239
W	ASP388
W	HOH2056

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	48
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
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)