Structure of PDB 1pxg Chain A

Receptor sequence
>1pxgA (length=365) Species: 542 (Zymomonas mobilis) [Search protein sequence]
RPRFSFSIAAREGKARTGTIEMKRGVIRTPAFMPVGTAATVKALKPETVR
ATGADIILGNTYHLMLRPGAERIAKLGGLHSFMGWDRPILTDSGGYQVMS
LSSLTKQSEEGVTFKSHLDGSRHMLSPERSIEIQHLLGSDIVMAFDECTP
YPATPSRAASSMERSMRWAKRSRDAFDSRKEQAENAALFGIQQGSVFENL
RQQSADALAEIGFDGYAVGGLAVGEGQDEMFRVLDFSVPMLPDDKPHYLM
GVGKPDDIVGAVERGIDMFECVGQAFTWDGPINIRNARFSEDLKPLDSEC
HCAVCQKWSRAYIHHLIRAGEILGAMLMTEHNIAFYQQLMQKIRDSISEG
RFSQFAQDFRARYFA
3D structure
PDB1pxg An essential role for aspartate 264 in catalysis by tRNA-guanine transglycosylase from Escherichia coli.
ChainA
Resolution1.7 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 E280 C318 C320 C323 H349
Catalytic site (residue number reindexed from 1) D92 E270 C300 C302 C305 H331
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 C300 C302 C305 H331
BS02 PRF A Y106 D156 C158 G229 G230 L231 M260 Y96 D146 C148 G219 G220 L221 M250
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:1pxg, PDBe:1pxg, PDBj:1pxg
PDBsum1pxg
PubMed12909636
UniProtP28720|TGT_ZYMMO Queuine tRNA-ribosyltransferase (Gene Name=tgt)

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