Target Information
| Target General Information | Top | |||||
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| Target ID |
T91001
(Former ID: TTDNC00628)
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| Target Name |
Bacterial Elongation factor Tu (Bact EFTu)
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| Synonyms |
tufA; P43; Elongation factor Tu 1; EFTu 1
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| Gene Name |
Bact EFTu
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| Target Type |
Literature-reported target
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[1] | ||||
| Function |
May play an important regulatory rolein cell growth and in the bacterial response to nutrient deprivation.
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| BioChemical Class |
GTP-binding elongation factor family
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| UniProt ID | ||||||
| Sequence |
MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARG
ITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHI LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALE GDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVG EEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIK PHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMV VTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLG Click to Show/Hide
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| 3D Structure | Click to Show 3D Structure of This Target | PDB | ||||
| Drug Binding Sites of Target | Top | |||||
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| Ligand Name: Tetracycline | Ligand Info | |||||
| Structure Description | Trypsin-modified Elongation Factor Tu in complex with tetracycline | PDB:2HCJ | ||||
| Method | X-ray diffraction | Resolution | 2.12 Å | Mutation | Yes | [2] |
| PDB Sequence |
> Chain A
TKPHVNVGTI 17 GHVDHGKTTL27 TAAITTVLAK37 TYG> Chain B GITINTSHVE 68 YDTPTRHYAH78 VDPGHADYVK89 NMITGAAQMD99 GAILVVAATD109 GPMPQTREHI 119 LLGRQVGVPY129 IIVFLNKCDM139 VDDEELLELV149 EMEVRELLSQ159 YDFPGDDTPI 169 VRGSALKALE179 GDAEWEAKIL189 ELAGFLDSYI199 PEPERAIDKP209 FLLPIEDVFS 219 ISGRGTVVTG229 RVERGIIKVG239 EEVEIVGIKE249 TQKSTCTGVE259 MFRKLLDEGR 269 AGENVGVLLR279 GIKREEIERG289 QVLAKPGTIK299 PHTKFESEVY309 ILSKDEGGRH 319 TPFFKGYRPQ329 FYFRTTDVTG339 TIELPEGVEM349 VMPGDNIKMV359 VTLIHPIAMD 369 DGLRFAIREG379 GRTVGAGVVA389 KVLG
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: Guanosine-5'-Diphosphate | Ligand Info | |||||
| Structure Description | Elongation factor Tu:Ts complex with partially bound GDP | PDB:4PC3 | ||||
| Method | X-ray diffraction | Resolution | 1.83 Å | Mutation | No | [3] |
| PDB Sequence |
TKPHVNVGTI
17 GHVDHGKTTL27 TAAITTVLAK37 TYGGSHVEYD70 TPTRHYAHVD80 CPGHADYVKN 90 MITGAAQMDG100 AILVVAATDG110 PMPQTREHIL120 LGRQVGVPYI130 IVFLNKCDMV 140 DDEELLELVE150 MEVRELLSQY160 DFPGDDTPIV170 RGSALKALEG180 DAEWEAKILE 190 LAGFLDSYIP200 EPERAIDKPF210 LLPIEDVFSI220 SGRGTVVTGR230 VERGIIKVGE 240 EVEIVGIKET250 QKSTCTGVEM260 FRKLLDEGRA270 GENVGVLLRG280 IKREEIERGQ 290 VLAKPGTIKP300 HTKFESEVYI310 LSKDEGGRHT320 PFFKGYRPQF330 YFRTTDVTGT 340 IELPEGVEMV350 MPGDNIKMVV360 TLIHPIAMDD370 GLRFAIREGG380 RTVGAGVVAK 390 VLG
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Click to View More Binding Site Information of This Target with Different Ligands | ||||||
| Different Human System Profiles of Target | Top |
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Human Similarity Proteins
of target is determined by comparing the sequence similarity of all human proteins with the target based on BLAST. The similarity proteins for a target are defined as the proteins with E-value < 0.005 and outside the protein families of the target.
A target that has fewer human similarity proteins outside its family is commonly regarded to possess a greater capacity to avoid undesired interactions and thus increase the possibility of finding successful drugs
(Brief Bioinform, 21: 649-662, 2020).
Human Similarity Proteins
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There is no similarity protein (E value < 0.005) for this target
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| Target Profiles in Patients | Top | |||||
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| Drug Resistance Mutation (DRM) | ||||||
| References | Top | |||||
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| REF 1 | In vitro and in vivo activities of novel, semisynthetic thiopeptide inhibitors of bacterial elongation factor Tu. Antimicrob Agents Chemother. 2011 Nov;55(11):5277-83. | |||||
| REF 2 | Molecular complementarity between tetracycline and the GTPase active site of elongation factor Tu. Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1392-400. | |||||
| REF 3 | Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu. J Struct Biol. 2015 Jul;191(1):10-21. | |||||
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