Structure of PDB 4fr1 Chain A

Receptor sequence
>4fr1A (length=337) Species: 264203 (Zymomonas mobilis subsp. mobilis ZM4 = ATCC 31821) [Search protein sequence]
RPRFSFSIAAREGKARTGTIEMKRGVIRTPAFMPVGADIILGNTYHLMLR
PGAERIAKLGGLHSFMGWDRPILTDSGGYQVMQSEEGVTFLSPERSIEIQ
HLLGSDIVMAFDECTPYPATPSRAASSMERSMRWAKRSRDAFDSRKEQAE
NAALFGIQQGSVFENLRQQSADALAEIGFDGYAVGGLAVGEGQDEMFRVL
DFSVPMLPDDKPHYLMGVGKPDDIVGAVERGIDMFDCVLPTRSGRNGQAF
TWDGPINIRNARFSEDLKPLDECHCAVCQKWSRAYIHHLIRAGEILGAML
MTEHNIAFYQQLMQKIRDSISEGRFSQFAQDFRARYF
3D structure
PDB4fr1 Studies on TGT homodimer interface
ChainA
Resolution1.74 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) D75 D236 C273 C275 C278 H304
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 C273 C275 C278 H304
BS02 0V2 A D102 Y106 D156 C158 G229 A232 M260 G261 D280 D75 Y79 D112 C114 G185 A188 M216 G217 D236
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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Cellular Component
External links
PDB RCSB:4fr1, PDBe:4fr1, PDBj:4fr1
PDBsum4fr1
PubMed
UniProtP28720|TGT_ZYMMO Queuine tRNA-ribosyltransferase (Gene Name=tgt)

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