Structure of PDB 1b23 Chain P Binding Site BS03

Receptor Information
>1b23 Chain P (length=405) Species: 271 (Thermus aquaticus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AKGEFIRTKPHVNVGTIGHVDHGKTTLTAALTYVAAAENPNVEVKDYGDI
DKAPEERARGITINTAHVEYETAKRHYSHVDCPGHADYIKNMITGAAQMD
GAILVVSAADGPMPQTREHILLARQVGVPYIVVFMNKVDMVDDPELLDLV
EMEVRDLLNQYEFPGDEVPVIRGSALLALEEMHKNPKTKRGENEWVDKIW
ELLDAIDEYIPTPVRDVDKPFLMPVEDVFTITGRGTVATGRIERGKVKVG
DEVEIVGLAPETRKTVVTGVEMHRKTLQEGIAGDNVGLLLRGVSREEVER
GQVLAKPGSITPHTKFEASVYILKKEEGGRHTGFFTGYRPQFYFRTTDVT
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 chain1b23 Chain P Residue 407 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1b23 The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA.
Resolution2.6 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) 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:1b23, PDBe:1b23, PDBj:1b23
PDBsum1b23
PubMed10368282
UniProtQ01698|EFTU_THEAQ Elongation factor Tu (Gene Name=tuf)

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