Structure of PDB 1efm Chain A

Receptor sequence
>1efmA (length=158) Species: 562 (Escherichia coli) [Search protein sequence]
VNVGTIGHVDHGKTTLTAAITTVLAKTYTINTSHVEYDTPTRHYAHVDCP
GHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIV
FLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDA
EWEAKILE
3D structure
PDB1efm Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins.
ChainA
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 T61 H84
Catalytic site (residue number reindexed from 1) D10 K13 T14 T29 H52
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 A V20 D21 G23 V9 D10 G12
Gene Ontology
Molecular Function
GO:0003723 RNA binding
GO:0003746 translation elongation factor activity
GO:0003924 GTPase activity
GO:0005515 protein binding
GO:0005525 GTP binding
GO:0097216 guanosine tetraphosphate binding
Biological Process
GO:0006412 translation
GO:0006414 translational elongation
GO:0046677 response to antibiotic
Cellular Component
GO:0005737 cytoplasm
GO:0005886 plasma membrane
GO:0032045 guanyl-nucleotide exchange factor complex

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Biological Process
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Cellular Component
External links
PDB RCSB:1efm, PDBe:1efm, PDBj:1efm
PDBsum1efm
PubMed3898365
UniProtP0CE48|EFTU2_ECOLI Elongation factor Tu 2 (Gene Name=tufB)

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