1EFM: Elongation factor tu

Structure of the GDP domain of ef-tu and location of the amino acids homologous to ras oncogene proteins. Determined by X-ray diffraction at 2.7 Å resolution. Released 16 Jul 1987.

Method
X-ray diffraction
Resolution
2.7 Å
Organism
Escherichia coli
Chains
1
Atoms
187
Mol. weight
42.12 kDa
Ligands
GDP, MG
Released
16 Jul 1987

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Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Elongation factor tuAprotein379Escherichia coliP0CE48 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1EFM_1 ELONGATION FACTOR TU (chains A)
SKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARGITINTSHVEYDTPTR
HYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFL
NKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKILELAGF
LDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKST
CTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKD
EGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRF
AIREGGRTVGAGVVAKVLS

Ligands and cofactors

IDNameFormulaCopies
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P21
MGMagnesium ionMg1

Primary citation

Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins. Jurnak, F. Science (1985) 230:32-36. PubMed

Other PDB entries of the same protein (UniProt P0CE48 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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