Structure of PDB 1y5x Chain D Binding Site BS01
Receptor Information
>1y5x Chain D (length=352) Species:
542
(Zymomonas mobilis) [
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RPRFSFSIAAREGKARTGTIEMKRGVIRTPAFMPVGTGADIILGNTYHLM
LRPGAERIAKLGGLHSFMGWDRPILTDSGGYQVMSLSSLTKQSEEGVTFK
SRHMLSPERSIEIQHLLGSDIVMAFDECTPYPATPSRAASSMERSMRWAK
RSRDAFDSRKEQAENAALFGIQQGSVFENLRQQSADALAEIGFDGYAVGG
LAVGEGQDEMFRVLDFSVPMLPDDKPHYLMGVGKPDDIVGAVERGIDMFD
CVLPTRSGRNGQAFTWDGPINIRNARFSEDLKPLDSECHCAVCQKWSRAY
IHHLIRAGEILGAMLMTEHNIAFYQQLMQKIRDSISEGRFSQFAQDFRAR
YF
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
1y5x Chain D Residue 1400 [
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Receptor-Ligand Complex Structure
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PDB
1y5x
Crystal structures of tRNA-guanine transglycosylase (TGT) in complex with novel and potent inhibitors unravel pronounced induced-fit adaptations and suggest dimer formation upon substrate binding
Resolution
2.1 Å
Binding residue
(original residue number in PDB)
C1318 C1320 C1323 H1349
Binding residue
(residue number reindexed from 1)
C288 C290 C293 H319
Annotation score
1
Enzymatic activity
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:1y5x
,
PDBe:1y5x
,
PDBj:1y5x
PDBsum
1y5x
PubMed
17524419
UniProt
P28720
|TGT_ZYMMO Queuine tRNA-ribosyltransferase (Gene Name=tgt)
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