Structure of PDB 4leq Chain A Binding Site BS01

Receptor Information
>4leq Chain A (length=373) Species: 264203 (Zymomonas mobilis subsp. mobilis ZM4 = ATCC 31821) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DRPRFSFSIAAREGKARTGTIEMKRGVIRTPAFMPVGTAATVKALKPETV
RATGADIILGNTYHLMLRPGAERIAKLGGLHSFMGWDRPILTDSGGYQVM
SLSSLTKQSEEGVTFKSLDGSRHMLSPERSIEIQHLLGSDIVMAFDECTP
YPATPSRAASSMERSMRWAKRSRDAFDSRKEQAENAALFGIQQGSVFENL
RQQSADALAEIGFDGYAVGGLAVGEGQDEMFRVLDFSVPMLPDDKPHYLM
GVGKPDDIVGAVERGIDMFDCVLPTRSGRNGQAFTWDGPINIRNARFSED
LKPLDSECHCAVCQKWSRAYIHHLIRAGEILGAMLMTEHNIAFYQQLMQK
IRDSISEGRFSQFAQDFRARYFA
Ligand information
Ligand ID1WK
InChIInChI=1S/C17H22N6O5/c1-19-17-20-8-5-7-10(21-16(18)23-14(7)26)6(11(8)22-17)3-4-9-12(24)13(25)15(27-2)28-9/h5,9,12-13,15,24-25H,3-4H2,1-2H3,(H2,19,20,22)(H3,18,21,23,26)/t9-,12-,13-,15-/m1/s1
InChIKeyVKQAJTKFJIETGO-QGMIFYJMSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6CNc1[nH]c2cc3c(c(c2n1)CC[C@@H]4[C@H]([C@H]([C@@H](O4)OC)O)O)N=C(NC3=O)N
CACTVS 3.385CNc1[nH]c2cc3C(=O)NC(=Nc3c(CC[CH]4O[CH](OC)[CH](O)[CH]4O)c2n1)N
ACDLabs 12.01O=C1NC(=Nc3c1cc2nc(nc2c3CCC4OC(OC)C(O)C4O)NC)N
CACTVS 3.385CNc1[nH]c2cc3C(=O)NC(=Nc3c(CC[C@H]4O[C@@H](OC)[C@H](O)[C@@H]4O)c2n1)N
OpenEye OEToolkits 1.7.6CNc1[nH]c2cc3c(c(c2n1)CCC4C(C(C(O4)OC)O)O)N=C(NC3=O)N
FormulaC17 H22 N6 O5
Namemethyl 6-[6-amino-2-(methylamino)-8-oxo-7,8-dihydro-1H-imidazo[4,5-g]quinazolin-4-yl]-5,6-dideoxy-beta-D-ribo-hexofuranoside
ChEMBL
DrugBank
ZINCZINC000263621127
PDB chain4leq Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4leq Replacement of Water Molecules in a Phosphate Binding Site by Furanoside-Appended lin-Benzoguanine Ligands of tRNA-Guanine Transglycosylase (TGT).
Resolution1.405 Å
Binding residue
(original residue number in PDB)		T47 L68 N70 D102 Y106 Q107 D156 C158 G229 L231 A232 M260 G261 D280
Binding residue
(residue number reindexed from 1)		T38 L59 N61 D93 Y97 Q98 D146 C148 G219 L221 A222 M250 G251 D270
Annotation score1
Binding affinityMOAD: Kd=288nM
PDBbind-CN: -logKd/Ki=6.54,Kd=288nM
Enzymatic activity
Catalytic site (original residue number in PDB) D102 D280 C318 C320 C323 H349
Catalytic site (residue number reindexed from 1) D93 D270 C308 C310 C313 H339
Enzyme Commision number 2.4.2.29: tRNA-guanosine(34) preQ1 transglycosylase.
Gene Ontology
Molecular Function
GO:0008479 tRNA-guanosine(34) queuine transglycosylase activity
GO:0016757 glycosyltransferase activity
GO:0016763 pentosyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0002099 tRNA wobble guanine modification
GO:0006400 tRNA modification
GO:0008033 tRNA processing
GO:0008616 queuosine biosynthetic process
GO:0101030 tRNA-guanine transglycosylation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4leq, PDBe:4leq, PDBj:4leq
PDBsum4leq
PubMed25483606
UniProtP28720|TGT_ZYMMO Queuine tRNA-ribosyltransferase (Gene Name=tgt)

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