Structure of PDB 1efc Chain A

Receptor sequence
>1efcA (length=386) Species: 562 (Escherichia coli) [Search protein sequence]
TKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKA
RGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAA
TDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELL
SQYDFPGDDTPIVRGSALKALEGDAEWEAKILELAGFLDSYIPEPERAID
KPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKSTCTG
VEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESE
VYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIK
MVVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLS
3D structure
PDB1efc Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05 A resolution.
ChainA
Resolution2.05 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) D14 K17 T18 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 A D21 G23 K24 T25 T26 F46 N135 K136 D138 M139 S173 L175 D14 G16 K17 T18 T19 F39 N128 K129 D131 M132 S166 L168
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1efc, PDBe:1efc, PDBj:1efc
PDBsum1efc
PubMed9918724
UniProtP0CE47|EFTU1_ECOLI Elongation factor Tu 1 (Gene Name=tufA)

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