Structure of PDB 1q2s Chain B Binding Site BS01
Receptor Information
>1q2s Chain B (length=372) Species:
542
(Zymomonas mobilis) [
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RPRFSFSIAAREGKARTGTIEMKRGVIRTPAFMPVGTAATVKALKPETVR
ATGADIILGNTYHLMLRPGAERIAKLGGLHSFMGWDRPILTDSGGYQVMS
LSSLTKQSEEGVTFKSHLDGSRHMLSPERSIEIQHLLGSDIVMAFDECTP
YPATPSRAASSMERSMRWAKRSRDAFDSRKEQAENAALFGIQQGSVFENL
RQQSADALAEIGFDGYAVGGLAVGEGQDEMFRVLDFSVPMLPDDKPHYLM
GVGKPDDIVGAVERGIDMFDCVLPTRSGRNGQAFTWDGPINIRNARFSED
LKPLDSECHCAVCQKWSRAYIHHLIRAGEILGAMLMTEHNIAFYQQLMQK
IRDSISEGRFSQFAQDFRARYF
Ligand information
>1q2s Chain E (length=20) [
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agcacggcuguaaaccgugc
.<<<<<<.......>>>>>>
Receptor-Ligand Complex Structure
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PDB
1q2s
Chemical trapping and crystal structure of a catalytic tRNA guanine transglycosylase covalent intermediate
Resolution
3.2 Å
Binding residue
(original residue number in PDB)
R77 L128 R289 I340
Binding residue
(residue number reindexed from 1)
R67 L118 R279 I330
Enzymatic activity
Catalytic site (original residue number in PDB)
D102 D280 C318 C320 C323 H349
Catalytic site (residue number reindexed from 1)
D92 D270 C308 C310 C313 H339
Enzyme Commision number
2.4.2.29
: tRNA-guanosine(34) preQ1 transglycosylase.
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:1q2s
,
PDBe:1q2s
,
PDBj:1q2s
PDBsum
1q2s
PubMed
12949492
UniProt
P28720
|TGT_ZYMMO Queuine tRNA-ribosyltransferase (Gene Name=tgt)
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