Structure of PDB 1it8 Chain B

Receptor sequence
>1it8B (length=577) Species: 53953 (Pyrococcus horikoshii) [Search protein sequence]
KMLKFEIKARDGAGRIGKLEVNGKKIETPAIMPVVNPKQMVVEPKELEKM
GFEIIITNSYIIYKDEELRRKALELGIHRMLDYNGIIEVDSGSFQLMKYG
SIEVSNREIIEFQHRIGVDIGTFLDIPTPPDAPREQAVKELEITLSRARE
AEEIKEIPMNATIQGSTYTDLRRYAARRLSSMNFEIHPIGGVVPLLESYR
FRDVVDIVISSKMALRPDRPVHLFGAGHPIVFALAVAMGVDLFDSASYAL
YAKDDRYMTPEGTKRLDELDYFPCSCPVCSKYTPQELREMPKEERTRLLA
LHNLWVIKEEIKRVKQAIKEGELWRLVDERARSHPKLYSAYKRLLEHYTF
LEEFEPITKKSALFKISNESLRWPVVRRAKERAKSINERFGELVEHPIFG
RVSRYLSLTYPFAQSEAEDDFKIEKPTKEDAIKYVMAIAEYQFGEGASRA
FDDAKVELSKTGMPRQVKVNGKRLATVRADDGLLTLGIEGAKRLHRVLPY
PRMRVVVNKEAEPFARKGKDVFAKFVIFADPGIRPYDEVLVVNENDELLA
TGQALLSGREMIVFQYGRAVKVRKGVE
3D structure
PDB1it8 Crystal structure of archaeosine tRNA-guanine transglycosylase.
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D95 D249 C279 C281 C284 H307
Catalytic site (residue number reindexed from 1) D90 D244 C274 C276 C279 H302
Enzyme Commision number 2.4.2.48: tRNA-guanine(15) 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 B C279 C281 C284 H307 C274 C276 C279 H302
BS02 MG B A528 I567 A523 I562
Gene Ontology
Molecular Function
GO:0003723 RNA binding
GO:0008270 zinc ion binding
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
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1it8, PDBe:1it8, PDBj:1it8
PDBsum1it8
PubMed12054814
UniProtO58843|ATGT_PYRHO tRNA-guanine(15) transglycosylase (Gene Name=tgtA)

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