Structure of PDB 5lpp Chain A

Receptor sequence
>5lppA (length=340) Species: 264203 (Zymomonas mobilis subsp. mobilis ZM4 = ATCC 31821) [Search protein sequence]
DRPRFSFSIAAREGKARTGTIEMKRGVIRTPAFMPVGTAATADIILGNTY
HLMLRPGAERIAKLGGLHSFMGWDRPILTDSGGYQSEEGVTFMLSPERSI
EIQHLLGSDIVMAFDECTPYPATPSRAASSMERSMRWAKRSRDAFDSRKE
QAENAALFGIQQGSVFENLRQQSADALAEIGFDGYAVGGLAVGEGQDEMF
RVLDFSVPMLPDDKPHYLMGVGKPDDIVGAVERGIDMFDCVLPTRSGRNG
QAFTWDGPINIRNARFSEDLKPLDCHCAVCQKWSRAYIHHLIRAGEILGA
MLMTEHNIAFYQQLMQKIRDSISEGRFSQFAQDFRARYFA
3D structure
PDB5lpp Carbohydrate-based Inhibitors targeting the Ribose-34 pocket of Z.mobilis TGT and changing the oligomeric state of the homodimer
ChainA
Resolution1.99 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 C318 C320 C323 H349
Catalytic site (residue number reindexed from 1) D80 D239 C275 C277 C280 H306
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 ZN A C318 C320 C323 H349 C275 C277 C280 H306
BS02 72C A L68 D102 Y106 D156 C158 G229 A232 M260 G261 L46 D80 Y84 D115 C117 G188 A191 M219 G220
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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Cellular Component
External links
PDB RCSB:5lpp, PDBe:5lpp, PDBj:5lpp
PDBsum5lpp
PubMed
UniProtP28720|TGT_ZYMMO Queuine tRNA-ribosyltransferase (Gene Name=tgt)

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