Structure of PDB 1eft Chain A Binding Site BS01

Receptor Information
>1eft Chain A (length=405) Species: 271 (Thermus aquaticus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AKGEFIRTKPHVNVGTIGHVDHGKTTLTAALTFVTAAENPNVEVKDYGDI
DKAPEERARGITINTAHVEYETAKRHYSHVDCPGHADYIKNMITGAAQMD
GAILVVSAADGPMPQTREHILLARQVGVPYIVVFMNKVDMVDDPELLDLV
EMEVRDLLNQYEFPGDEVPVIRGSALLALEEMHKNPKTKRGENEWVDKIW
ELLDAIDEYIPTPVRDVDKPFLMPVEDVFTITGRGTVATGRIERGKVKVG
DEVEIVGLAPETRKTVVTGVEMHRKTLQEGIAGDNVGLLLRGVSREEVER
GQVLAKPGSITPHTKFEASVYVLKKEEGGRHTGFFSGYRPQFYFRTTDVT
GVVRLPQGVEMVMPGDNVTFTVELIKPVALEEGLRFAIREGGRTVGAGVV
TKILE
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain1eft Chain A Residue 407 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1eft The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		T25 T62
Binding residue
(residue number reindexed from 1)		T25 T62
Annotation score1
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 ?
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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