Structure of PDB 5i07 Chain B Binding Site BS02

Receptor Information
>5i07 Chain B (length=368) 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]
RPRFSFSIAAREGKARTGTIEMKRGVIRTPAFMPVGTAATVRATGADIIL
GNTYHLMLRPGAERIAKLGGLHSFMGWDRPILTDSGGYQVMSLSSLTKQS
EEGVTFKSHLDGSRHMLSPERSIEIQHLLGSDIVMAFDECTPYPATPSRA
ASSMERSMRWAKRSRDAFDSRKEQAENAALFGIQQGSVFENLRQQSADAL
AEIGFDGYAVGGLAVGEGQDEMFRVLDFSVPMLPDDKPHYLMGVGKPDDI
VGAVERGIDMFDCVLPTRSGRNGQAFTWDGPINIRNARFSEDLKPLDSEC
HCAVCQKWSRAYIHHLIRAGEILGAMLMTEHNIAFYQQLMQKIRDSISEG
RFSQFAQDFRARYFARNS
Ligand information
Ligand IDNE8
InChIInChI=1S/C17H15N5O/c18-17-21-14-11(7-6-10-4-2-1-3-5-10)15-13(19-9-20-15)8-12(14)16(23)22-17/h1-5,8-9H,6-7H2,(H,19,20)(H3,18,21,22,23)
InChIKeyPBZAIUVFRISTSZ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1ccc(cc1)CCc2c3c(cc4c2N=C(NC4=O)N)[nH]cn3
CACTVS 3.341NC1=Nc2c(CCc3ccccc3)c4nc[nH]c4cc2C(=O)N1
ACDLabs 10.04O=C1NC(=Nc3c1cc2c(ncn2)c3CCc4ccccc4)N
FormulaC17 H15 N5 O
Name6-AMINO-4-(2-PHENYLETHYL)-1,7-DIHYDRO-8H-IMIDAZO[4,5-G]QUINAZOLIN-8-ONE
ChEMBL
DrugBankDB08267
ZINCZINC000033836604
PDB chain5i07 Chain B Residue 403 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5i07 Co-crystallization, Isothermal titration calorimetry and nanoESI-MS reveal dimer disturbing inhibitors
Resolution1.89 Å
Binding residue
(original residue number in PDB)		L68 D102 Y106 D156 C158 G229 L231 A232 M260 G261 D280
Binding residue
(residue number reindexed from 1)		L50 D84 Y88 D138 C140 G211 L213 A214 M242 G243 D262
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) D102 D280 C318 C320 C323 H349
Catalytic site (residue number reindexed from 1) D84 D262 C300 C302 C305 H331
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5i07, PDBe:5i07, PDBj:5i07
PDBsum5i07
PubMed
UniProtP28720|TGT_ZYMMO Queuine tRNA-ribosyltransferase (Gene Name=tgt)

[Back to BioLiP]