Structure of PDB 4fsa Chain A

Receptor sequence
>4fsaA (length=347) Species: 264203 (Zymomonas mobilis subsp. mobilis ZM4 = ATCC 31821) [Search protein sequence]
RPRFSFSIAAREGKARTGTIEMKRGVIRTPAFMPVGATVKALKPETVRAT
GADIILGNTYHLMLRPGAERIAKLGGLHSFMGWDRPILTDSGYQSEEGVT
LSPERSIEIQHLLGSDIVMAFDETPYPATPSRAASSMERSMRWAKRSRDA
FDSRKEQAENAALFGIQQGSVFENLRQQSADALAEIGFDGYAVGGLAVGE
GQDEMFRVLDFSVPMLPDDKPHYLMGVGKPDDIVGAVERGIDMFDCVLPT
RSGRNGQAFTWDGPINIRNARFSEDLKPLDSECHCAVCQKWSRAYIHHLI
RAGEILGAMLMTEHNIAFYQQLMQKIRDSISEGRFSQFAQDFRARYF
3D structure
PDB4fsa Studies on TGT homodimer interface
ChainA
Resolution1.62 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) D90 D245 C283 C285 C288 H314
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 C283 C285 C288 H314
BS02 0V3 A D102 Y106 D156 G229 L231 A232 M260 G261 D280 D90 Y93 D122 G194 L196 A197 M225 G226 D245
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:4fsa, PDBe:4fsa, PDBj:4fsa
PDBsum4fsa
PubMed
UniProtP28720|TGT_ZYMMO Queuine tRNA-ribosyltransferase (Gene Name=tgt)

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