Structure of PDB 5wdt Chain z Binding Site BS06
Receptor Information
>5wdt Chain z (length=393) Species:
562
(Escherichia coli) [
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SKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQID
NAPEEKARGITINTSHVEYDTPTRHYAHVDCPGAADYVKNMITGAAQMDG
AILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVE
MEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKILELAGFLDSYIP
EPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKET
QKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKP
HTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMV
MPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLS
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
5wdt Chain z Residue 404 [
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Receptor-Ligand Complex Structure
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PDB
5wdt
Cryo-EM shows stages of initial codon selection on the ribosome by aa-tRNA in ternary complex with GTP and the GTPase-deficient EF-TuH84A.
Resolution
3.0 Å
Binding residue
(original residue number in PDB)
T25 T61
Binding residue
(residue number reindexed from 1)
T25 T61
Annotation score
1
Enzymatic activity
Enzyme Commision number
?
Gene Ontology
Molecular Function
GO:0003723
RNA binding
GO:0003746
translation elongation factor activity
GO:0003924
GTPase activity
GO:0005515
protein binding
GO:0005525
GTP binding
GO:0097216
guanosine tetraphosphate binding
Biological Process
GO:0006412
translation
GO:0006414
translational elongation
GO:0046677
response to antibiotic
Cellular Component
GO:0005737
cytoplasm
GO:0005886
plasma membrane
GO:0032045
guanyl-nucleotide exchange factor complex
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:5wdt
,
PDBe:5wdt
,
PDBj:5wdt
PDBsum
5wdt
PubMed
29733411
UniProt
P0CE48
|EFTU2_ECOLI Elongation factor Tu 2 (Gene Name=tufB)
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