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5D0B

Crystal structure of epoxyqueuosine reductase with a tRNA-TYR epoxyqueuosine-modified tRNA stem loop

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006400biological_processtRNA modification
A0008033biological_processtRNA processing
A0008616biological_processtRNA queuosine(34) biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
A0052693molecular_functionepoxyqueuosine reductase activity
B0005737cellular_componentcytoplasm
B0006400biological_processtRNA modification
B0008033biological_processtRNA processing
B0008616biological_processtRNA queuosine(34) biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
B0051536molecular_functioniron-sulfur cluster binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
B0052693molecular_functionepoxyqueuosine reductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue SF4 A 501
ChainResidue
AALA153
ALYS154
AASN155
ACYS188
ACYS191
ACYS194
ACYS247
ALEU249

site_idAC2
Number of Residues7
Detailsbinding site for residue SF4 A 502
ChainResidue
ALEU209
ACYS214
AILE215
ACYS240
ATHR242
ACYS243
ACYS198

site_idAC3
Number of Residues30
Detailsbinding site for residue B12 A 503
ChainResidue
ALEU33
AARG36
ASER47
AGLU50
AARG57
ACYS97
AASP134
ALEU138
ASER139
AASP140
AARG141
AALA142
ASER152
AASN155
AMET157
AILE158
ASER165
AVAL167
ALEU169
APRO206
AGLY207
ALEU209
ASER216
AGLY239
ACYS240
AASP241
AGLN244
AHOH607
AHOH608
F56B34

site_idAC4
Number of Residues3
Detailsbinding site for residue PO4 A 504
ChainResidue
ALYS112
AHIS258
AGLU260

site_idAC5
Number of Residues6
Detailsbinding site for residue GOL A 505
ChainResidue
AASN280
AGLY296
ALYS297
FC32
FA36
FHOH106

site_idAC6
Number of Residues9
Detailsbinding site for residue SF4 B 501
ChainResidue
BALA153
BLYS154
BASN155
BCYS188
BCYS191
BCYS194
BCYS247
BPRO248
BLEU249

site_idAC7
Number of Residues7
Detailsbinding site for residue SF4 B 502
ChainResidue
BCYS198
BLEU209
BCYS214
BILE215
BCYS240
BTHR242
BCYS243

site_idAC8
Number of Residues36
Detailsbinding site for residue B12 B 503
ChainResidue
BGLY239
BCYS240
BASP241
BCYS243
BGLN244
BHOH614
BHOH619
AGLU373
BSER32
BLEU33
BARG36
BLEU37
BSER47
BGLU50
BARG57
BCYS97
BTYR105
BASP134
BLEU138
BSER139
BASP140
BARG141
BALA142
BSER152
BASN155
BCYS156
BMET157
BILE158
BSER165
BVAL167
BLEU169
BPRO206
BGLY207
BLEU209
BSER216
BPHE217

site_idAC9
Number of Residues5
Detailsbinding site for residue PO4 B 504
ChainResidue
BILE17
BLYS112
BLEU257
BHIS258
BGLU260

Functional Information from PROSITE/UniProt
site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CgSCTkCLdACP
ChainResidueDetails
ACYS188-PRO199

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues60
DetailsDomain: {"description":"4Fe-4S ferredoxin-type","evidences":[{"source":"HAMAP-Rule","id":"MF_00916","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues48
DetailsRepeat: {"description":"HEAT-like PBS-type"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"27638883","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues38
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27638883","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5D0B","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27638883","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

244693

PDB entries from 2025-11-12

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