Structure of PDB 1eft Chain A

Receptor sequence
>1eftA (length=405) Species: 271 (Thermus aquaticus) [Search protein sequence]
AKGEFIRTKPHVNVGTIGHVDHGKTTLTAALTFVTAAENPNVEVKDYGDI
DKAPEERARGITINTAHVEYETAKRHYSHVDCPGHADYIKNMITGAAQMD
GAILVVSAADGPMPQTREHILLARQVGVPYIVVFMNKVDMVDDPELLDLV
EMEVRDLLNQYEFPGDEVPVIRGSALLALEEMHKNPKTKRGENEWVDKIW
ELLDAIDEYIPTPVRDVDKPFLMPVEDVFTITGRGTVATGRIERGKVKVG
DEVEIVGLAPETRKTVVTGVEMHRKTLQEGIAGDNVGLLLRGVSREEVER
GQVLAKPGSITPHTKFEASVYVLKKEEGGRHTGFFSGYRPQFYFRTTDVT
GVVRLPQGVEMVMPGDNVTFTVELIKPVALEEGLRFAIREGGRTVGAGVV
TKILE
3D structure
PDB1eft The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation.
ChainA
Resolution2.5 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) D21 K24 T25 T62 H85
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 MG A T25 T62 T25 T62
BS02 GNP A V20 D21 G23 K24 T25 T26 Y47 I61 T62 G84 N136 K137 D139 M140 S174 L176 V20 D21 G23 K24 T25 T26 Y47 I61 T62 G84 N136 K137 D139 M140 S174 L176
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:1eft, PDBe:1eft, PDBj:1eft
PDBsum1eft
PubMed8069622
UniProtQ01698|EFTU_THEAQ Elongation factor Tu (Gene Name=tuf)

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