Structure of PDB 5lps Chain A

Receptor sequence
>5lpsA (length=341) Species: 264203 (Zymomonas mobilis subsp. mobilis ZM4 = ATCC 31821) [Search protein sequence]
RPRFSFSIAAREGKARTGTIEMKRGVIRTPAFMPVGTAATGADIILGNTY
HLMLRPGAERIAKLGGLHSFMGWDRPILTDSGGYQSEEGVTFKSHLDGSR
HMLSPERSIEIQHLLGSDIVMAFDECTPYPATPSRAASSMERSMRWAKRS
RDAFDSRKEQAENAALFGIQQGSVFENLRQQSADALAEIGFDGYAVGGLA
VGEGQDEMFRVLDFSVPMLPDDKPHYLMGVGKPDDIVGAVERGIDMFDCV
LPTRSNGQAFTWDGPINIRNARFSEDLKPLDSKWSRAYIHHLIRAGEILG
AMLMTEHNIAFYQQLMQKIRDSISEGRFSQFAQDFRARYFA
3D structure
PDB5lps Carbohydrate-based Inhibitors targeting the Ribose-34 pocket of Z.mobilis TGT and changing the oligomeric state of the homodimer
ChainA
Resolution1.27 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D102 D280 H349
Catalytic site (residue number reindexed from 1) D80 D248 H307
Enzyme Commision number 2.4.2.29: tRNA-guanosine(34) preQ1 transglycosylase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 726 A L68 N70 D102 Y106 D156 C158 G229 A232 M260 G261 D280 L46 N48 D80 Y84 D124 C126 G197 A200 M228 G229 D248
BS02 ZN A D315 H349 D281 H307
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:5lps, PDBe:5lps, PDBj:5lps
PDBsum5lps
PubMed
UniProtP28720|TGT_ZYMMO Queuine tRNA-ribosyltransferase (Gene Name=tgt)

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