Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5D0A

Crystal structure of epoxyqueuosine reductase with cleaved RNA stem loop

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0006400	biological_process	tRNA modification
A	0008033	biological_process	tRNA processing
A	0008616	biological_process	tRNA queuosine(34) biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
A	0052693	molecular_function	epoxyqueuosine reductase activity
B	0005737	cellular_component	cytoplasm
B	0006400	biological_process	tRNA modification
B	0008033	biological_process	tRNA processing
B	0008616	biological_process	tRNA queuosine(34) biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0046872	molecular_function	metal ion binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	0052693	molecular_function	epoxyqueuosine reductase activity
C	0005737	cellular_component	cytoplasm
C	0006400	biological_process	tRNA modification
C	0008033	biological_process	tRNA processing
C	0008616	biological_process	tRNA queuosine(34) biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0046872	molecular_function	metal ion binding
C	0051536	molecular_function	iron-sulfur cluster binding
C	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	0052693	molecular_function	epoxyqueuosine reductase activity
D	0005737	cellular_component	cytoplasm
D	0006400	biological_process	tRNA modification
D	0008033	biological_process	tRNA processing
D	0008616	biological_process	tRNA queuosine(34) biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0046872	molecular_function	metal ion binding
D	0051536	molecular_function	iron-sulfur cluster binding
D	0051539	molecular_function	4 iron, 4 sulfur cluster binding
D	0052693	molecular_function	epoxyqueuosine reductase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue SF4 A 501

Chain	Residue
A	ALA153
A	LYS154
A	ASN155
A	CYS188
A	CYS191
A	CYS194
A	CYS247
A	LEU249

site_id	AC2
Number of Residues	8
Details	binding site for residue SF4 A 502

Chain	Residue
A	PRO199
A	LEU209
A	CYS214
A	ILE215
A	CYS240
A	THR242
A	CYS243
A	CYS198

site_id	AC3
Number of Residues	38
Details	binding site for residue B12 A 503

Chain	Residue
A	SER32
A	LEU33
A	ARG36
A	SER47
A	PHE49
A	GLU50
A	ARG57
A	CYS97
A	ASP134
A	LEU138
A	SER139
A	ASP140
A	ARG141
A	ALA142
A	SER152
A	ASN155
A	CYS156
A	MET157
A	ILE158
A	SER165
A	VAL167
A	LEU169
A	PRO206
A	LEU209
A	SER216
A	PHE217
A	GLY239
A	CYS240
A	ASP241
A	CYS243
A	GLN244
A	HOH630
A	HOH632
A	HOH635
A	HOH652
A	HOH683
A	HOH692
A	HOH747

site_id	AC4
Number of Residues	7
Details	binding site for residue GOL A 504

Chain	Residue
A	PHE49
A	ASP134
A	GLN220
A	TYR238
A	TRP294
A	HOH652
A	HOH653

site_id	AC5
Number of Residues	6
Details	binding site for residue PO4 A 505

Chain	Residue
A	LYS112
A	HIS258
A	PRO259
A	GLU260
A	HOH639
A	HOH682

site_id	AC6
Number of Residues	7
Details	binding site for residue SF4 B 501

Chain	Residue
B	ALA153
B	LYS154
B	ASN155
B	CYS188
B	CYS191
B	CYS194
B	CYS247

site_id	AC7
Number of Residues	8
Details	binding site for residue SF4 B 502

Chain	Residue
B	CYS198
B	LEU203
B	LEU209
B	CYS214
B	ILE215
B	CYS240
B	THR242
B	CYS243

site_id	AC8
Number of Residues	35
Details	binding site for residue B12 B 503

Chain	Residue
B	SER165
B	VAL167
B	LEU169
B	PRO206
B	GLY207
B	LEU209
B	SER216
B	GLY239
B	CYS240
B	ASP241
B	CYS243
B	GLN244
B	HOH616
B	HOH628
B	HOH640
B	HOH643
B	HOH668
B	HOH677
B	SER32
B	LEU33
B	ARG36
B	SER47
B	GLU50
B	ARG57
B	CYS97
B	ASP134
B	LEU138
B	SER139
B	ASP140
B	ARG141
B	SER152
B	ASN155
B	CYS156
B	MET157
B	ILE158

site_id	AC9
Number of Residues	6
Details	binding site for residue GOL B 504

Chain	Residue
B	ASP134
B	GLN220
B	TYR238
B	TRP294
B	HOH657
B	HOH677

site_id	AD1
Number of Residues	4
Details	binding site for residue PO4 B 505

Chain	Residue
B	LYS112
B	HIS258
B	PRO259
B	GLU260

site_id	AD2
Number of Residues	7
Details	binding site for residue SF4 C 501

Chain	Residue
C	ALA153
C	LYS154
C	ASN155
C	CYS188
C	CYS191
C	CYS194
C	CYS247

site_id	AD3
Number of Residues	7
Details	binding site for residue SF4 C 502

Chain	Residue
C	CYS198
C	LEU209
C	CYS214
C	ILE215
C	CYS240
C	THR242
C	CYS243

site_id	AD4
Number of Residues	38
Details	binding site for residue B12 C 503

Chain	Residue
C	SER32
C	LEU33
C	ARG36
C	SER47
C	PHE49
C	GLU50
C	ARG57
C	CYS97
C	ASP134
C	LEU138
C	SER139
C	ASP140
C	ARG141
C	GLU145
C	SER152
C	ASN155
C	CYS156
C	MET157
C	ILE158
C	SER165
C	VAL167
C	LEU169
C	PRO206
C	GLY207
C	LEU209
C	SER216
C	PHE217
C	GLY239
C	CYS240
C	ASP241
C	CYS243
C	GLN244
C	HOH642
C	HOH648
C	HOH657
C	HOH673
C	HOH678
C	HOH692

site_id	AD5
Number of Residues	7
Details	binding site for residue GOL C 504

Chain	Residue
C	PHE49
C	ASP134
C	GLN220
C	TYR238
C	TRP294
C	HOH653
C	HOH678

site_id	AD6
Number of Residues	4
Details	binding site for residue PO4 C 505

Chain	Residue
C	LYS112
C	HIS258
C	PRO259
C	GLU260

site_id	AD7
Number of Residues	8
Details	binding site for residue SF4 D 501

Chain	Residue
D	ALA153
D	LYS154
D	ASN155
D	CYS188
D	CYS191
D	CYS194
D	CYS247
D	LEU249

site_id	AD8
Number of Residues	6
Details	binding site for residue SF4 D 502

Chain	Residue
D	CYS198
D	LEU209
D	CYS214
D	ILE215
D	CYS240
D	CYS243

site_id	AD9
Number of Residues	36
Details	binding site for residue B12 D 503

Chain	Residue
D	SER32
D	LEU33
D	ARG36
D	SER47
D	GLU50
D	ARG57
D	CYS97
D	ASP134
D	LEU138
D	SER139
D	ASP140
D	ARG141
D	ALA142
D	SER152
D	ASN155
D	CYS156
D	ILE158
D	SER165
D	VAL167
D	LEU169
D	PRO206
D	GLY207
D	LEU209
D	SER216
D	GLY239
D	CYS240
D	ASP241
D	CYS243
D	GLN244
D	HOH614
D	HOH648
D	HOH655
D	HOH666
D	HOH678
D	HOH693
D	HOH744

site_id	AE1
Number of Residues	7
Details	binding site for residue GOL D 504

Chain	Residue
D	PHE49
D	ASP134
D	GLN220
D	TYR238
D	TRP294
D	HOH628
D	HOH693

site_id	AE2
Number of Residues	5
Details	binding site for residue PO4 D 505

Chain	Residue
D	LYS112
D	HIS258
D	PRO259
D	GLU260
D	HOH659

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. CgSCTkCLdACP

Chain	Residue	Details
A	CYS188-PRO199

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	120
Details	Domain: {"description":"4Fe-4S ferredoxin-type","evidences":[{"source":"HAMAP-Rule","id":"MF_00916","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	96
Details	Repeat: {"description":"HEAT-like PBS-type"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"27638883","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	76
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27638883","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5D0B","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27638883","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)