Structure of PDB 2ash Chain A

Receptor sequence
>2ashA (length=361) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MEFEVKKTFGKARLGVMKLHHGAVETPVFMPVGTNASVKLLTPRDLEEAG
AEIILSNTFHLMLKPGVEIIKLHRGLHNFMGWKRPILTDSGGFQVFSLPK
IRIDDEGVVFRSPIDGSKVFLNPEISMEVQIALGSDICMVFDHCPVADYE
EVKEATERTYRWALRSKKAFKTENQALFGIVQGGIYPDLRRESALQLTSI
GFDGYAIGGLSIGEERSLTLEMTEVTVEFLPEDKPRYFMGGGSPELILEL
VDRGVDMFDSVFPTRIARHGTALTWNGKLNLKASYNKRSLEPVDERCGCY
TCKNFTRSYIHHLFDRGEVLGQILLTIHNINFMISLMKEVRRSIESGTFK
ELKSKVVEVYS
3D structure
PDB2ash Crystal structure of Queuine tRNA-ribosyltransferase (EC 2.4.2.29) (tRNA-guanine (tm1561) from THERMOTOGA MARITIMA at 1.90 A resolution
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D89 D261 C299 C301 C304 H330
Catalytic site (residue number reindexed from 1) D89 D259 C297 C299 C302 H328
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 C299 C301 C304 H330 C297 C299 C302 H328
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:2ash, PDBe:2ash, PDBj:2ash
PDBsum2ash
PubMed
UniProtQ9X1P7|TGT_THEMA Queuine tRNA-ribosyltransferase (Gene Name=tgt)

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