2B1X

Crystal structure of naphthalene 1,2-dioxygenase from Rhodococcus sp.

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	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	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	0051213	molecular_function	dioxygenase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 502

Chain	Residue
A	HIS216
A	HIS221
A	ASP372
A	HOH1961
A	HOH1962

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE C 502

Chain	Residue
C	HOH1958
C	HIS216
C	HIS221
C	ASP372
C	HOH1957

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE E 502

Chain	Residue
E	HIS216
E	HIS221
E	ASP372
E	HOH2010
E	HOH2011

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES A 501

Chain	Residue
A	CYS88
A	HIS90
A	ARG91
A	CYS108
A	HIS111
A	GLY112
A	TRP113

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES C 501

Chain	Residue
C	CYS88
C	HIS90
C	ARG91
C	CYS108
C	TYR110
C	HIS111
C	TRP113

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES E 501

Chain	Residue
E	CYS88
E	HIS90
E	ARG91
E	CYS108
E	HIS111
E	TRP113

---

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MPD A 1700

Chain	Residue
A	ASP213
A	HIS216
A	THR217
A	HIS221
A	HIS295
A	PHE362
A	HOH1962

---

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MPD C 1701

Chain	Residue
A	ARG222
C	ARG107
C	PRO125

---

site_id	AC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MPD A 1702

Chain	Residue
A	GLU226

---

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MPD A 1703

Chain	Residue
A	GLU374
A	ARG377
A	ARG381
B	ARG632
B	GLY633
B	VAL635
C	GLN94

---

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MPD C 1704

Chain	Residue
C	ASP213
C	ALA214
C	HIS216
C	THR217
C	HIS295
C	HOH1958

---

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MPD E 1705

Chain	Residue
C	MET218
C	ARG222
E	ARG107

---

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MPD C 1707

Chain	Residue
C	GLU374
C	ARG377
C	ARG381
D	ARG632
D	GLY633
D	VAL635
E	GLN94

---

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MPD E 1708

Chain	Residue
E	ASP213
E	ALA214
E	HIS216
E	THR217
E	HIS295
E	HOH2010

---

site_id	BC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MPD A 1709

Chain	Residue
A	ARG107
E	ARG222

---

site_id	BC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MPD E 1710

Chain	Residue
E	VAL225

---

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MPD E 1711

Chain	Residue
A	GLN94
E	GLU374
E	ARG377
E	SER378
E	ARG381
F	ARG632
F	GLY633

---

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD E 1712

Chain	Residue
E	PRO231
E	MET260
E	PHE293
E	HOH1778
E	HOH1838

---

site_id	CC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MPD E 1713

Chain	Residue
E	TYR61
E	VAL95
E	CYS96
E	ARG97
E	ALA98
E	HOH1807
E	HOH1911
F	GLU560

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	CYS88-HIS111

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	HIS111
E	HIS216
E	ASP213

---

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

Chain	Residue	Details
A	HIS216
A	ASP213
C	HIS111

---

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

Chain	Residue	Details
C	HIS216
C	ASP213
E	HIS111

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