Structure of PDB 1ttt Chain A Binding Site BS02
Receptor Information
>1ttt Chain A (length=405) Species:
271
(Thermus aquaticus) [
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AKGEFIRTKPHVNVGTIGHVDHGKTTLTAALTYVAAAENPNVEVKDYGDI
DKAPEERARGITINTAHVEYETAKRHYSHVDCPGHADYIKNMITGAAQMD
GAILVVSAADGPMPQTREHILLARQVGVPYIVVFMNKVDMVDDPELLDLV
EMEVRDLLNQYEFPGDEVPVIRGSALLALEEMHKNPKTKRGENEWVDKIW
ELLDAIDEYIPTPVRDVDKPFLMPVEDVFTITGRGTVATGRIERGKVKVG
DEVEIVGLAPETRKTVVTGVEMHRKTLQEGIAGDNVGLLLRGVSREEVER
GQVLAKPGSITPHTKFEASVYILKKEEGGRHTGFFTGYRPQFYFRTTDVT
GVVRLPQGVEMVMPGDNVTFTVELIKPVALEEGLRFAIREGGRTVGAGVV
TKILE
Ligand information
>1ttt Chain F (length=76) [
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gcggauuuagcucaguugggagagcgccagacugaagaucuggagguccu
guguucgauccacagaauucgcacca
<<<<<<<..<<<<........>>>>.<<<<<.......>>>>>.....<<
<<<.......>>>>>>>>>>>>....
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)
F335 T336 E360 E405
Binding residue
(residue number reindexed from 1)
F335 T336 E360 E405
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
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Molecular Function
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Biological Process
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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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