4NBA

Carbazole-bound oxygenase with Ile262 replaced by Val and ferredoxin complex of carbazole 1,9a-dioxygenase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0046872	molecular_function	metal ion binding
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0046872	molecular_function	metal ion binding
B	0051537	molecular_function	2 iron, 2 sulfur cluster binding
C	0046872	molecular_function	metal ion binding
C	0051537	molecular_function	2 iron, 2 sulfur cluster binding
D	0008901	molecular_function	ferredoxin hydrogenase activity
D	0046232	biological_process	carbazole catabolic process
D	0046872	molecular_function	metal ion binding
D	0051213	molecular_function	dioxygenase activity
D	0051537	molecular_function	2 iron, 2 sulfur cluster binding
E	0008901	molecular_function	ferredoxin hydrogenase activity
E	0046232	biological_process	carbazole catabolic 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	0008901	molecular_function	ferredoxin hydrogenase activity
F	0046232	biological_process	carbazole catabolic process
F	0046872	molecular_function	metal ion binding
F	0051213	molecular_function	dioxygenase activity
F	0051537	molecular_function	2 iron, 2 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 A 501

Chain	Residue
A	HIS183
A	HIS187
A	ASP333
A	HOH625

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES A 502

Chain	Residue
A	TYR92
A	HIS93
A	TRP95
A	CYS69
A	HIS71
A	ARG72
A	VAL74
A	CYS90

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 B 501

Chain	Residue
B	HIS183
B	HIS187
B	ASP333
B	HOH821

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES B 502

Chain	Residue
B	CYS69
B	HIS71
B	ARG72
B	CYS90
B	TYR92
B	HIS93
B	TRP95

---

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 9CA B 503

Chain	Residue
B	GLY178
B	ALA259
B	LEU270
B	VAL272
B	PHE275
B	GLN282
B	GLU284
B	PHE329
B	ASN330
B	HOH821
B	HOH822

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 C 501

Chain	Residue
C	HIS183
C	HIS187
C	ASP333
C	HOH647

---

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES C 502

Chain	Residue
C	CYS69
C	HIS71
C	ARG72
C	VAL74
C	CYS90
C	TYR92
C	HIS93
C	TRP95

---

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 9CA C 503

Chain	Residue
C	GLY178
C	ALA259
C	LEU270
C	VAL272
C	PHE275
C	GLN282
C	GLU284
C	PHE329
C	ASN330
C	HOH647
C	HOH792

---

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES D 201

Chain	Residue
D	CYS46
D	HIS48
D	GLY49
D	CYS65
D	PHE67
D	HIS68
D	GLY70

---

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES E 201

Chain	Residue
E	CYS46
E	HIS48
E	GLY49
E	CYS65
E	HIS68
E	GLY70

---

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES F 201

Chain	Residue
F	CYS46
F	HIS48
F	GLY49
F	CYS65
F	PHE67
F	HIS68
F	GLY70

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000269|PubMed:15645447, ECO:0000269|PubMed:17161368

Chain	Residue	Details
D	CYS46
F	HIS48
F	CYS65
F	HIS68
D	HIS48
D	CYS65
D	HIS68
E	CYS46
E	HIS48
E	CYS65
E	HIS68
F	CYS46

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