Structure of PDB 1ttt Chain C Binding Site BS04
Receptor Information
>1ttt Chain C (length=405) Species:
271
(Thermus aquaticus) [
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AKGEFIRTKPHVNVGTIGHVDHGKTTLTAALTYVAAAENPNVEVKDYGDI
DKAPEERARGITINTAHVEYETAKRHYSHVDCPGHADYIKNMITGAAQMD
GAILVVSAADGPMPQTREHILLARQVGVPYIVVFMNKVDMVDDPELLDLV
EMEVRDLLNQYEFPGDEVPVIRGSALLALEEMHKNPKTKRGENEWVDKIW
ELLDAIDEYIPTPVRDVDKPFLMPVEDVFTITGRGTVATGRIERGKVKVG
DEVEIVGLAPETRKTVVTGVEMHRKTLQEGIAGDNVGLLLRGVSREEVER
GQVLAKPGSITPHTKFEASVYILKKEEGGRHTGFFTGYRPQFYFRTTDVT
GVVRLPQGVEMVMPGDNVTFTVELIKPVALEEGLRFAIREGGRTVGAGVV
TKILE
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
1ttt Chain C Residue 407 [
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Receptor-Ligand Complex Structure
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PDB
1ttt
Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog.
Resolution
2.7 Å
Binding residue
(original residue number in PDB)
T25 D51 T62
Binding residue
(residue number reindexed from 1)
T25 D51 T62
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
K24 T25 T62 H85
Catalytic site (residue number reindexed from 1)
K24 T25 T62 H85
Enzyme Commision number
?
Gene Ontology
Molecular Function
GO:0003746
translation elongation factor activity
GO:0003924
GTPase activity
GO:0005525
GTP binding
Biological Process
GO:0006412
translation
GO:0006414
translational elongation
Cellular Component
GO:0005737
cytoplasm
GO:0005829
cytosol
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:1ttt
,
PDBe:1ttt
,
PDBj:1ttt
PDBsum
1ttt
PubMed
7491491
UniProt
Q01698
|EFTU_THEAQ Elongation factor Tu (Gene Name=tuf)
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