5XBP

Oxygenase component of 3-nitrotoluene dioxygenase from Diaphorobacter sp. strain DS2

Replaces:  5BRC

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0016491	molecular_function	oxidoreductase activity
A	0019439	biological_process	obsolete aromatic compound catabolic process
A	0044237	biological_process	cellular metabolic process
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
C	0006725	biological_process	obsolete cellular aromatic compound metabolic process
C	0019380	biological_process	3-phenylpropionate catabolic process
D	0005506	molecular_function	iron ion binding
D	0016491	molecular_function	oxidoreductase activity
D	0019439	biological_process	obsolete aromatic compound catabolic process
D	0044237	biological_process	cellular metabolic process
D	0046872	molecular_function	metal ion binding
D	0051213	molecular_function	dioxygenase activity
D	0051536	molecular_function	iron-sulfur cluster binding
D	0051537	molecular_function	2 iron, 2 sulfur cluster binding
F	0006725	biological_process	obsolete cellular aromatic compound metabolic process
F	0019380	biological_process	3-phenylpropionate catabolic process
G	0005506	molecular_function	iron ion binding
G	0016491	molecular_function	oxidoreductase activity
G	0019439	biological_process	obsolete aromatic compound catabolic process
G	0044237	biological_process	cellular metabolic process
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
I	0006725	biological_process	obsolete cellular aromatic compound metabolic process
I	0019380	biological_process	3-phenylpropionate catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue FE A 501

Chain	Residue
A	HIS206
A	HIS211
A	ASP360

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site_id	AC2
Number of Residues	5
Details	binding site for residue FES A 502

Chain	Residue
A	CYS79
A	HIS81
A	ARG82
A	CYS99
A	HIS102

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site_id	AC3
Number of Residues	4
Details	binding site for residue FE D 501

Chain	Residue
D	HIS211
D	ASP360
D	HOH608
D	HIS206

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site_id	AC4
Number of Residues	5
Details	binding site for residue FES D 502

Chain	Residue
D	CYS79
D	HIS81
D	ARG82
D	CYS99
D	HIS102

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site_id	AC5
Number of Residues	3
Details	binding site for residue FE G 501

Chain	Residue
G	HIS206
G	HIS211
G	ASP360

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site_id	AC6
Number of Residues	6
Details	binding site for residue FES G 502

Chain	Residue
G	CYS79
G	HIS81
G	ARG82
G	CYS99
G	TYR101
G	HIS102

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site_id	AC7
Number of Residues	12
Details	binding site for Di-peptide TYR G 167 and PRO G 398

Chain	Residue
G	ASP163
G	ALA164
G	ALA165
G	TRP166
G	MET168
G	GLU169
G	PRO170
G	MET240
G	MET248
G	TYR397
G	GLY399
G	VAL401

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	CYS79-HIS102

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