5D6S

Structure of epoxyqueuosine reductase from Streptococcus thermophilus.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0008033	biological_process	tRNA processing
A	0008616	biological_process	queuosine biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
A	0052693	molecular_function	epoxyqueuosine reductase activity
B	0005737	cellular_component	cytoplasm
B	0008033	biological_process	tRNA processing
B	0008616	biological_process	queuosine biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0046872	molecular_function	metal ion binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	0052693	molecular_function	epoxyqueuosine reductase activity
C	0005737	cellular_component	cytoplasm
C	0008033	biological_process	tRNA processing
C	0008616	biological_process	queuosine biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0046872	molecular_function	metal ion binding
C	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	0052693	molecular_function	epoxyqueuosine reductase activity
D	0005737	cellular_component	cytoplasm
D	0008033	biological_process	tRNA processing
D	0008616	biological_process	queuosine biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0046872	molecular_function	metal ion binding
D	0051539	molecular_function	4 iron, 4 sulfur cluster binding
D	0052693	molecular_function	epoxyqueuosine reductase activity
E	0005737	cellular_component	cytoplasm
E	0008033	biological_process	tRNA processing
E	0008616	biological_process	queuosine biosynthetic process
E	0016491	molecular_function	oxidoreductase activity
E	0046872	molecular_function	metal ion binding
E	0051539	molecular_function	4 iron, 4 sulfur cluster binding
E	0052693	molecular_function	epoxyqueuosine reductase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue SF4 A 401

Chain	Residue
A	LYS150
A	CYS184
A	CYS187
A	ARG188
A	CYS190
A	CYS243
A	PRO244

---

site_id	AC2
Number of Residues	7
Details	binding site for residue SF4 A 402

Chain	Residue
A	MET205
A	CYS210
A	LEU211
A	CYS236
A	CYS239
A	CYS194
A	CYS198

---

site_id	AC3
Number of Residues	30
Details	binding site for residue B12 A 403

Chain	Residue
A	LEU30
A	THR44
A	ARG54
A	THR93
A	ASN95
A	ASP130
A	LEU134
A	VAL135
A	ASP136
A	THR137
A	LYS141
A	ILE148
A	ASN151
A	GLY152
A	LEU153
A	VAL154
A	SER161
A	MET163
A	LEU165
A	ASP202
A	GLY203
A	THR204
A	MET205
A	SER212
A	GLY235
A	CYS236
A	ASP237
A	GLN240
A	HOH506
A	HOH518

---

site_id	AC4
Number of Residues	7
Details	binding site for residue SF4 B 401

Chain	Residue
B	LYS150
B	CYS184
B	CYS187
B	ARG188
B	CYS190
B	CYS243
B	PRO244

---

site_id	AC5
Number of Residues	7
Details	binding site for residue SF4 B 402

Chain	Residue
B	CYS194
B	CYS198
B	MET205
B	CYS210
B	LEU211
B	CYS236
B	CYS239

---

site_id	AC6
Number of Residues	27
Details	binding site for residue B12 B 403

Chain	Residue
B	LEU30
B	LEU34
B	ARG54
B	THR93
B	ASN95
B	ASP130
B	LEU134
B	ASP136
B	THR137
B	ILE148
B	ASN151
B	GLY152
B	LEU153
B	VAL154
B	SER161
B	MET163
B	LEU165
B	GLY203
B	THR204
B	MET205
B	SER212
B	GLY235
B	CYS236
B	ASP237
B	CYS239
B	GLN240
B	HOH508

---

site_id	AC7
Number of Residues	6
Details	binding site for residue SF4 C 401

Chain	Residue
C	LYS150
C	CYS184
C	CYS187
C	CYS190
C	CYS243
C	PRO244

---

site_id	AC8
Number of Residues	7
Details	binding site for residue SF4 C 402

Chain	Residue
C	CYS194
C	CYS198
C	LEU199
C	CYS210
C	LEU211
C	CYS236
C	CYS239

---

site_id	AC9
Number of Residues	29
Details	binding site for residue B12 C 403

Chain	Residue
C	LEU34
C	ARG54
C	THR93
C	ASN95
C	ASP130
C	LEU134
C	ASP136
C	THR137
C	LYS141
C	ILE148
C	ASN151
C	GLY152
C	LEU153
C	VAL154
C	SER161
C	MET163
C	LEU165
C	ASP202
C	GLY203
C	THR204
C	MET205
C	SER212
C	GLY235
C	CYS236
C	ASP237
C	GLN240
C	HOH509
C	HOH512
C	LEU30

---

site_id	AD1
Number of Residues	8
Details	binding site for residue SF4 D 401

Chain	Residue
D	GLY149
D	LYS150
D	CYS184
D	CYS187
D	ARG188
D	CYS190
D	CYS243
D	PRO244

---

site_id	AD2
Number of Residues	7
Details	binding site for residue SF4 D 402

Chain	Residue
D	CYS194
D	CYS198
D	MET205
D	CYS210
D	LEU211
D	CYS236
D	CYS239

---

site_id	AD3
Number of Residues	32
Details	binding site for residue B12 D 403

Chain	Residue
D	LEU30
D	SER33
D	LEU34
D	ARG54
D	THR93
D	ASN95
D	TYR101
D	ASP130
D	LEU134
D	ASP136
D	THR137
D	LYS141
D	ILE148
D	ASN151
D	GLY152
D	LEU153
D	VAL154
D	SER161
D	MET163
D	LEU165
D	ASP202
D	GLY203
D	THR204
D	MET205
D	SER212
D	GLY235
D	CYS236
D	ASP237
D	CYS239
D	GLN240
D	HOH501
D	HOH503

---

site_id	AD4
Number of Residues	7
Details	binding site for residue SF4 E 401

Chain	Residue
E	LYS150
E	CYS184
E	CYS187
E	ARG188
E	CYS190
E	CYS243
E	PRO244

---

site_id	AD5
Number of Residues	7
Details	binding site for residue SF4 E 402

Chain	Residue
E	CYS194
E	CYS198
E	MET205
E	CYS210
E	LEU211
E	CYS236
E	CYS239

---

site_id	AD6
Number of Residues	28
Details	binding site for residue B12 E 403

Chain	Residue
E	LEU30
E	LEU34
E	THR44
E	ARG54
E	THR93
E	ASN95
E	ASP130
E	LEU134
E	ASP136
E	THR137
E	LYS141
E	ILE148
E	ASN151
E	GLY152
E	VAL154
E	SER161
E	MET163
E	LEU165
E	GLY203
E	THR204
E	MET205
E	SER212
E	CYS236
E	CYS239
E	GLN240
E	HOH502
E	HOH505
E	HOH507

---

Functional Information from PROSITE/UniProt

site_id	PS00198
Number of Residues	12
Details	4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CgDCRrCLdACP

Chain	Residue	Details
A	CYS184-PRO195

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