2GBW

Crystal Structure of Biphenyl 2,3-Dioxygenase from Sphingomonas yanoikuyae B1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0009056	biological_process	catabolic process
A	0044237	biological_process	cellular metabolic process
A	0046872	molecular_function	metal ion binding
A	0051213	molecular_function	dioxygenase activity
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0019380	biological_process	3-phenylpropionate catabolic process
B	0046872	molecular_function	metal ion binding
B	0051213	molecular_function	dioxygenase activity
C	0005506	molecular_function	iron ion binding
C	0009056	biological_process	catabolic process
C	0044237	biological_process	cellular metabolic process
C	0046872	molecular_function	metal ion binding
C	0051213	molecular_function	dioxygenase activity
C	0051537	molecular_function	2 iron, 2 sulfur cluster binding
D	0019380	biological_process	3-phenylpropionate catabolic process
D	0046872	molecular_function	metal ion binding
D	0051213	molecular_function	dioxygenase activity
E	0005506	molecular_function	iron ion binding
E	0009056	biological_process	catabolic process
E	0044237	biological_process	cellular metabolic process
E	0046872	molecular_function	metal ion binding
E	0051213	molecular_function	dioxygenase activity
E	0051537	molecular_function	2 iron, 2 sulfur cluster binding
F	0019380	biological_process	3-phenylpropionate catabolic process
F	0046872	molecular_function	metal ion binding
F	0051213	molecular_function	dioxygenase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 456

Chain	Residue
A	HIS207
A	HIS212
A	ASP360
A	OXY457
A	HOH959

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE C 456

Chain	Residue
E	HOH811
C	HIS207
C	HIS212
C	ASP360
E	OXY457

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE E 456

Chain	Residue
C	OXY457
C	HOH898
E	HIS207
E	HIS212
E	ASP360

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES A 455

Chain	Residue
A	CYS80
A	HIS82
A	ARG83
A	CYS100
A	HIS103
A	TRP105

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE OXY A 457

Chain	Residue
A	ASN200
A	HIS207
A	HIS212
A	PHE350
A	ASP360
A	FE456
A	HOH663

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES C 455

Chain	Residue
C	CYS80
C	HIS82
C	ARG83
C	CYS100
C	HIS103
C	TRP105

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE OXY C 457

Chain	Residue
E	ASN200
E	HIS207
E	HIS212
E	PHE350
E	ASP360
E	FE456

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES E 455

Chain	Residue
E	CYS80
E	HIS82
E	ARG83
E	CYS100
E	HIS103
E	TRP105

---

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE OXY E 457

Chain	Residue
C	ASN200
C	HIS207
C	HIS212
C	PHE350
C	ASP360
C	FE456
C	HOH675

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	CYS80-HIS103

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1ndo

Chain	Residue	Details
A	HIS103
E	HIS207
E	ASP204

---

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1ndo

Chain	Residue	Details
A	ASP204
A	HIS207
C	HIS103

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ndo

Chain	Residue	Details
C	ASP204
C	HIS207
E	HIS103

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