Structure of PDB 1tui Chain C

Receptor sequence
>1tuiC (length=397) Species: 271 (Thermus aquaticus) [Search protein sequence]
KPHVNVGTIGHVDHGKTTLTAALTYVAAAENPNVEVKDYGDIDKAPEERA
RGITINTAHVEYETAKRHYSHVDCPGHADYIKNMITGAAQMDGAILVVSA
ADGPMPQTREHILLARQVGVPYIVVFMNKVDMVDDPELLDLVEMEVRDLL
NQYEFPGDEVPVIRGSALLALEEMHKNPKTKRGENEWVDKIWELLDAIDE
YIPTPVRDVDKPFLMPVEDVFTITGRGTVATGRIERGKVKVGDEVEIVGL
APETRKTVVTGVEMHRKTLQEGIAGDNVGLLLRGVSREEVERGQVLAKPG
SITPHTKFEASVYILKKEEGGRHTGFFTGYRPQFYFRTTDVTGVVRLPQG
VEMVMPGDNVTFTVELIKPVALEEGLRFAIREGGRTVGAGVVTKILE
3D structure
PDB1tui Helix unwinding in the effector region of elongation factor EF-Tu-GDP.
ChainC
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D21 K24 T25 T62 H85
Catalytic site (residue number reindexed from 1) D13 K16 T17 T54 H77
Enzyme Commision number ?
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 GDP C D21 G23 K24 T25 T26 Y47 N136 K137 D139 S174 L176 D13 G15 K16 T17 T18 Y39 N128 K129 D131 S166 L168
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:1tui, PDBe:1tui, PDBj:1tui
PDBsum1tui
PubMed8939739
UniProtQ01698|EFTU_THEAQ Elongation factor Tu (Gene Name=tuf)

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