Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T91001 | Target Info | |||
| Target Name | Bacterial Elongation factor Tu (Bact EFTu) | ||||
| Synonyms | tufA; P43; Elongation factor Tu 1; EFTu 1 | ||||
| Target Type | Literature-reported Target | ||||
| Gene Name | Bact EFTu | ||||
| Biochemical Class | GTP-binding elongation factor family | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Guanosine-5'-Diphosphate | Ligand Info | |||
| Canonical SMILES | C1=NC2=C(N1C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N=C(NC2=O)N | ||||
| InChI | 1S/C10H15N5O11P2/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(25-9)1-24-28(22,23)26-27(19,20)21/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1 | ||||
| InChIKey | QGWNDRXFNXRZMB-UUOKFMHZSA-N | ||||
| PubChem Compound ID | 135398619 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 4PC3 Elongation factor Tu:Ts complex with partially bound GDP | ||||||
| Method | X-ray diffraction | Resolution | 1.83 Å | Mutation | No | [1] |
| 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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| PDB ID: 5JBQ EF-TU (ESCHERICHIA COLI) IN COMPLEX WITH THIOMURACIN ANALOG | ||||||
| Method | X-ray diffraction | Resolution | 2.01 Å | Mutation | No | [2] |
| PDB Sequence |
KEKFERTKPH
11 VNVGTIGHVD21 HGKTTLTAAI31 TTVLAKTYGG41 AARAFDQIDN51 APEEKARGIT 61 INTSHVEYDT71 PTRHYAHVDC81 PGHADYVKNM91 ITGAAQMDGA101 ILVVAATDGP 111 MPQTREHILL121 GRQVGVPYII131 VFLNKCDMVD141 DEELLELVEM151 EVRELLSQYD 161 FPGDDTPIVR171 GSALKALEGD181 AEWEAKILEL191 AGFLDSYIPE201 PERAIDKPFL 211 LPIEDVFSIS221 GRGTVVTGRV231 ERGIIKVGEE241 VEIVGIKETQ251 KSTCTGVEMF 261 RKLLDEGRAG271 ENVGVLLRGI281 KREEIERGQV291 LAKPGTIKPH301 TKFESEVYIL 311 SKDEGGRHTP321 FFKGYRPQFY331 FRTTDVTGTI341 ELPEGVEMVM351 PGDNIKMVVT 361 LIHPIAMDDG371 LRFAIREGGR381 TVGAGVVAKV391 LG
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HIS19
3.868
VAL20
3.952
ASP21
2.919
HIS22
3.382
GLY23
3.100
LYS24
2.770
THR25
2.892
THR26
2.693
LEU27
4.979
PHE46
3.420
ASP50
4.944
|
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| PDB ID: 3U6B Ef-tu (escherichia coli) in complex with nvp-ldi028 | ||||||
| Method | X-ray diffraction | Resolution | 2.12 Å | Mutation | No | [3] |
| PDB Sequence |
FERTKPHVNV
14 GTIGHVDHGK24 TTLTAAITTV34 LAKTYGGRGI60 TINTSHVEYD70 TPTRHYAHVD 80 CPGHADYVKN90 MITGAAQMDG100 AILVVAATDG110 PMPQTREHIL120 LGRQVGVPYI 130 IVFLNKCDMV140 DDEELLELVE150 MEVRELLSQY160 DFPGDDTPIV170 RGSALKALEG 180 DAEWEAKILE190 LAGFLDSYIP200 EPERAIDKPF210 LLPIEDVFSI220 TVVTGRVERG 234 IIKVGEEVEI244 VGIKETQKST254 CTGVEMFRKL264 LDEGRAGENV274 GVLLRGIKRE 284 EIERGQVLAK294 PGTIKPHTKF304 ESEVYILSKD314 EGGRHTPFFK324 GYRPQFYFRT 334 TDVTGTIELP344 EGVEMVMPGD354 NIKMVVTLIH364 PIAMDDGLRF374 AIREGGRTVG 384 AGVVAKVLG
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| PDB ID: 4G5G ef-tu (Escherichia coli) complexed with nvp-ldu796 | ||||||
| Method | X-ray diffraction | Resolution | 2.30 Å | Mutation | No | [4] |
| PDB Sequence |
EKFERTKPHV
12 NVGTIGHVDH22 GKTTLTAAIT32 TVLAKTYGGA42 ARAFDQIDNA52 PEEKARGITI 62 NTSHVEYDTP72 TRHYAHVDCP82 GHADYVKNMI92 TGAAQMDGAI102 LVVAATDGPM 112 PQTREHILLG122 RQVGVPYIIV132 FLNKCDMVDD142 EELLELVEME152 VRELLSQYDF 162 PGDDTPIVRG172 SALKALEGDA182 EWEAKILELA192 GFLDSYIPEP202 ERAIDKPFLL 212 PIEDVFSISG222 RGTVVTGRVE232 RGIIKVGEEV242 EIVGIKETQK252 STCTGVEMFR 262 KLLDEGRAGE272 NVGVLLRGIK282 REEIERGQVL292 AKPGTIKPHT302 KFESEVYILS 312 KDEGGRHTPF322 FKGYRPQFYF332 RTTDVTGTIE342 LPEGVEMVMP352 GDNIKMVVTL 362 IHPIAMDDGL372 RFAIREGGRT382 VGAGVVAKVL392 G
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;style chemicals stick;color identity;select .A:19 or .A:20 or .A:21 or .A:22 or .A:23 or .A:24 or .A:25 or .A:26 or .A:27 or .A:46 or .A:50 or .A:80 or .A:82 or .A:135 or .A:136 or .A:137 or .A:138 or .A:139 or .A:172 or .A:173 or .A:174 or .A:175 or .A:176; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS19
3.772
VAL20
3.707
ASP21
2.692
HIS22
3.405
GLY23
2.935
LYS24
2.679
THR25
2.908
THR26
2.628
LEU27
4.831
PHE46
3.281
ASP50
4.920
ASP80
4.838
|
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| PDB ID: 3U6K Ef-tu (escherichia coli) in complex with nvp-ldk733 | ||||||
| Method | X-ray diffraction | Resolution | 2.45 Å | Mutation | No | [3] |
| PDB Sequence |
TKPHVNVGTI
17 GHVDHGKTTL27 TAAITTVLAK37 TYGGAARAFD47 QIDNAPEEKA57 RGITINTSHV 67 EYDTPTRHYA77 HVDCPGHADY87 VKNMITGAAQ97 MDGAILVVAA107 TDGPMPQTRE 117 HILLGRQVGV127 PYIIVFLNKC137 DMVDDEELLE147 LVEMEVRELL157 SQYDFPGDDT 167 PIVRGSALKA177 LEGDAEWEAK187 ILELAGFLDS197 YIPEPERAID207 KPFLLPIEDV 217 FSISGRGTVV227 TGRVERGIIK237 VGEEVEIVGI247 KETQKSTCTG257 VEMFRKLLDE 267 GRAGENVGVL277 LRGIKREEIE287 RGQVLAKPGT297 IKPHTKFESE307 VYILSKDEGG 317 RHTPFFKGYR327 PQFYFRTTDV337 TGTIELPEGV347 EMVMPGDNIK357 MVVTLIHPIA 367 MDDGLRFAIR377 EGGRTVGAGV387 VAKVLG
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|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;style chemicals stick;color identity;select .A:19 or .A:20 or .A:21 or .A:22 or .A:23 or .A:24 or .A:25 or .A:26 or .A:27 or .A:46 or .A:80 or .A:135 or .A:136 or .A:137 or .A:138 or .A:139 or .A:172 or .A:173 or .A:174 or .A:175; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| PDB ID: 3U2Q EF-Tu (Escherichia coli) in complex with NVP-LFF571 | ||||||
| Method | X-ray diffraction | Resolution | 2.70 Å | Mutation | No | [5] |
| PDB Sequence |
ERTKPHVNVG
15 TIGHVDHGKT25 TLTAAITTVL35 AKTYGGAARA45 FDQIDNAPEE55 KATINTSHVE 68 YDTPTRHYAH78 VDCPGHADYV88 KNMITGAAQM98 DGAILVVAAT108 DGPMPQTREH 118 ILLGRQVGVP128 YIIVFLNKCD138 MVDDEELLEL148 VEMEVRELLS158 QYDFPGDDTP 168 IVRGSALKAL178 EGDAEWEAKI188 LELAGFLDSY198 IPEPERAIDK208 PFLLPIEDVF 218 SISGRGTVVT228 GRVERGIIKV238 GEEVEIVGIK248 ETQKSTCTGV258 EMFRKLLDEG 268 RAGENVGVLL278 RGIKREEIER288 GQVLAKPGTI298 KPHTKFESEV308 YILSKDEGGR 318 HTPFFKGYRP328 QFYFRTTDVT338 GTIELPEGVE348 MVMPGDNIKM358 VVTLIHPIAM 368 DDGLRFAIRE378 GGRTVGAGVV388 AKVLG
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|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;style chemicals stick;color identity;select .A:19 or .A:20 or .A:21 or .A:22 or .A:23 or .A:24 or .A:25 or .A:26 or .A:27 or .A:46 or .A:50 or .A:80 or .A:82 or .A:135 or .A:136 or .A:137 or .A:138 or .A:139 or .A:172 or .A:173 or .A:174 or .A:175; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS19
3.622
VAL20
3.664
ASP21
2.748
HIS22
2.482
GLY23
2.764
LYS24
2.858
THR25
2.694
THR26
2.642
LEU27
4.811
PHE46
3.137
ASP50
3.391
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| PDB ID: 1EFC INTACT ELONGATION FACTOR FROM E.COLI | ||||||
| Method | X-ray diffraction | Resolution | 2.05 Å | Mutation | No | [6] |
| PDB Sequence |
TKPHVNVGTI
17 GHVDHGKTTL27 TAAITTVLAK37 TYGGAARAFD47 QIDNAPEEKA57 RGITINTSHV 67 EYDTPTRHYA77 HVDCPGHADY87 VKNMITGAAQ97 MDGAILVVAA107 TDGPMPQTRE 117 HILLGRQVGV127 PYIIVFLNKC137 DMVDDEELLE147 LVEMEVRELL157 SQYDFPGDDT 167 PIVRGSALKA177 LEGDAEWEAK187 ILELAGFLDS197 YIPEPERAID207 KPFLLPIEDV 217 FSISGRGTVV227 TGRVERGIIK237 VGEEVEIVGI247 KETQKSTCTG257 VEMFRKLLDE 267 GRAGENVGVL277 LRGIKREEIE287 RGQVLAKPGT297 IKPHTKFESE307 VYILSKDEGG 317 RHTPFFKGYR327 PQFYFRTTDV337 TGTIELPEGV347 EMVMPGDNIK357 MVVTLIHPIA 367 MDDGLRFAIR377 EGGRTVGAGV387 VAKVLS
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;style chemicals stick;color identity;select .A:19 or .A:20 or .A:21 or .A:22 or .A:23 or .A:24 or .A:25 or .A:26 or .A:27 or .A:46 or .A:50 or .A:80 or .A:135 or .A:136 or .A:138 or .A:139 or .A:172 or .A:173 or .A:174 or .A:175 or .A:176; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS19
3.851
VAL20
3.842
ASP21
2.784
HIS22
3.322
GLY23
2.861
LYS24
2.626
THR25
2.895
THR26
2.764
LEU27
4.873
PHE46
3.492
ASP50
4.825
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| PDB ID: 1D8T CRYSTAL STRUCTURE OF ELONGATION FACTOR, TU (EF-TU-MGGDP) COMPLEXED WITH GE2270A, A THIAZOLYL PEPTIDE ANTIBIOTIC | ||||||
| Method | X-ray diffraction | Resolution | 2.35 Å | Mutation | No | [7] |
| PDB Sequence |
EKFERTKPHV
12 NVGTIGHVDH22 GKTTLTAAIT32 TVLAKTYGGA42 ARAFDQIDNA52 PEEKARGITI 62 NTSHVEYDTP72 TRHYAHVDCP82 GHADYVKNMI92 TGAAQMDGAI102 LVVAATDGPM 112 PQTREHILLG122 RQVGVPYIIV132 FLNKCDMVDD142 EELLELVEME152 VRELLSQYDF 162 PGDDTPIVRG172 SALKALEGDA182 EWEAKILELA192 GFLDSYIPEP202 ERAIDKPFLL 212 PIEDVFSISG222 RGTVVTGRVE232 RGIIKVGEEV242 EIVGIKETQK252 STCTGVEMFR 262 KLLDEGRAGE272 NVGVLLRGIK282 REEIERGQVL292 AKPGTIKPHT302 KFESEVYILS 312 KDEGGRHTPF322 FKGYRPQFYF332 RTTDVTGTIE342 LPEGVEMVMP352 GDNIKMVVTL 362 IHPIAMDDGL372 RFAIREGGRT382 VGAGVVAKVL392 G
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;style chemicals stick;color identity;select .A:19 or .A:20 or .A:21 or .A:22 or .A:23 or .A:24 or .A:25 or .A:26 or .A:46 or .A:50 or .A:80 or .A:82 or .A:135 or .A:136 or .A:137 or .A:138 or .A:139 or .A:172 or .A:173 or .A:174 or .A:175 or .A:176; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS19
3.788
VAL20
3.934
ASP21
2.900
HIS22
3.549
GLY23
3.053
LYS24
2.661
THR25
2.876
THR26
2.775
PHE46
3.450
ASP50
4.755
ASP80
4.986
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| PDB ID: 1ETU STRUCTURAL DETAILS OF THE BINDING OF GUANOSINE DIPHOSPHATE TO ELONGATION FACTOR TU FROM E. COLI AS STUDIED BY X-RAY CRYSTALLOGRAPHY | ||||||
| Method | X-ray diffraction | Resolution | 2.90 Å | Mutation | No | [8] |
| PDB Sequence |
FERTKPHVNV
14 GTIGHVDHGK24 TTLTAAITTV34 LAKTYGITIN63 TSHVEYDTPT73 RHYAHVDCPG 83 HADYVKNMIT93 GAAQMDGAIL103 VVAATDGPMP113 QTREHILLGR123 QVGVPYIIVF 133 LNKCDMVDDE143 ELLELVEMEV153 RELLSQYDFP163 GDDTPIVRGS173 ALKALEGDAE 183 WEAKILELAG193 FLDSYIP
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;style chemicals stick;color identity;select .A:18 or .A:19 or .A:20 or .A:21 or .A:22 or .A:23 or .A:24 or .A:25 or .A:26 or .A:27 or .A:80 or .A:135 or .A:136 or .A:138 or .A:139 or .A:173 or .A:174 or .A:175; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| PDB ID: 2FX3 Crystal Structure Determination of E. coli Elongation Factor, Tu using a Twinned Data Set | ||||||
| Method | X-ray diffraction | Resolution | 3.40 Å | Mutation | No | [9] |
| PDB Sequence |
RTKPHVNVGT
16 IGHVDHGKTT26 LTAAITTVLA36 KTYGGAARAF46 DQIDNAPEEK56 ARGITINTSH 66 VEYDTPTRHY76 AHVDCPGHAD86 YVKNMITGAA96 QMDGAILVVA106 ATDGPMPQTR 116 EHILLGRQVG126 VPYIIVFLNK136 CDMVDDEELL146 ELVEMEVREL156 LSQYDFPGDD 166 TPIVRGSALK176 ALEGDAEWEA186 KILELAGFLD196 SYIPEPERAI206 DKPFLLPIED 216 VFSISGRGTV226 VTGRVERGII236 KVGEEVEIVG246 IKETQKSTCT256 GVEMFRKLLD 266 EGRAGENVGV276 LLRGIKREEI286 ERGQVLAKPG296 TIKPHTKFES306 EVYILSKDEG 316 GRHTPFFKGY326 RPQFYFRTTD336 VTGTIELPEG346 VEMVMPGDNI356 KMVVTLIHPI 366 AMDDGLRFAI376 REGGRTVGAG386 VVAKVLG
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;style chemicals stick;color identity;select .A:19 or .A:20 or .A:21 or .A:22 or .A:23 or .A:24 or .A:25 or .A:26 or .A:27 or .A:46 or .A:135 or .A:136 or .A:137 or .A:138 or .A:139 or .A:172 or .A:173 or .A:174 or .A:175 or .A:176; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| PDB ID: 2HCJ Trypsin-modified Elongation Factor Tu in complex with tetracycline | ||||||
| Method | X-ray diffraction | Resolution | 2.12 Å | Mutation | Yes | [10] |
| 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 Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;style chemicals stick;color identity;select .A:19 or .A:20 or .A:21 or .A:22 or .A:23 or .A:24 or .A:25 or .A:26 or .B:80 or .B:82 or .B:135 or .B:136 or .B:138 or .B:139 or .B:172 or .B:173 or .B:174 or .B:175 or .B:176; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS19[A]
3.847
VAL20[A]
3.941
ASP21[A]
2.861
HIS22[A]
3.491
GLY23[A]
3.120
LYS24[A]
2.646
THR25[A]
2.954
THR26[A]
2.779
ASP80[B]
4.927
PRO82[B]
4.859
|
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| PDB ID: 2HDN Trypsin-modified Elongation Factor Tu in complex with tetracycline at 2.8 Angstrom resolution | ||||||
| Method | X-ray diffraction | Resolution | 2.80 Å | Mutation | Yes | [10] |
| PDB Sequence |
> Chain A
TKPHVNVGTI 17 GHVDHGKTTL27 TAAITTVLAK37 TYG> Chain B GITINTSHVE 68 YDTPTRHYAH78 VDCPGHADYV88 KNMITGAAQM98 DGAILVVAAT108 DGPMPQTREH 118 ILLGRQVGVP128 YIIVFLNKCD138 MVDDEELLEL148 VEMEVRELLS158 QYDFPGDDTP 168 IVRGSALKAL178 EGDAEWEAKI188 LELAGFLDSY198 IPEPERAIDK208 PFLLPIEDVF 218 SISGRGTVVT228 GRVERGIIKV238 GEEVEIVGIK248 ETQKSTCTGV258 EMFRKLLDEG 268 RAGENVGVLL278 RGIKREEIER288 GQVLAKPGTI298 KPHTKFESEV308 YILSKDEGGR 318 HTPFFKGYRP328 QFYFRTTDVT338 GTIELPEGVE348 MVMPGDNIKM358 VVTLIHPIAM 368 DDGLRFAIRE378 GGRTVGAGVV388 AKVLG
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDP or .GDP2 or .GDP3 or :3GDP;style chemicals stick;color identity;select .A:19 or .A:20 or .A:21 or .A:22 or .A:23 or .A:24 or .A:25 or .A:26 or .A:27 or .B:82 or .B:135 or .B:136 or .B:137 or .B:138 or .B:139 or .B:172 or .B:173 or .B:174 or .B:175 or .B:176; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS19[A]
3.931
VAL20[A]
3.943
ASP21[A]
2.840
HIS22[A]
3.593
GLY23[A]
3.035
LYS24[A]
2.894
THR25[A]
2.688
THR26[A]
2.814
LEU27[A]
4.966
PRO82[B]
4.877
|
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | 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. | ||||
| REF 2 | Antibacterial and Solubility Optimization of Thiomuracin A. J Med Chem. 2016 Jul 28;59(14):6920-8. | ||||
| REF 3 | Antibacterial optimization of 4-aminothiazolyl analogues of the natural product GE2270 A: identification of the cycloalkylcarboxylic acids. J Med Chem. 2011 Dec 8;54(23):8099-109. | ||||
| REF 4 | Antibiotic optimization and chemical structure stabilization of thiomuracin A. J Med Chem. 2012 Aug 9;55(15):6934-41. | ||||
| REF 5 | Discovery of LFF571: an investigational agent for Clostridium difficile infection. J Med Chem. 2012 Mar 8;55(5):2376-87. | ||||
| REF 6 | Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05 A resolution. J Mol Biol. 1999 Jan 22;285(3):1245-56. | ||||
| REF 7 | Structure of an EF-Tu complex with a thiazolyl peptide antibiotic determined at 2.35 A resolution: atomic basis for GE2270A inhibition of EF-Tu. Biochemistry. 2000 Jan 11;39(1):37-45. | ||||
| REF 8 | Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography. EMBO J. 1985 Sep;4(9):2385-8. | ||||
| REF 9 | Solving the structure of Escherichia coli elongation factor Tu using a twinned data set. Acta Crystallogr D Biol Crystallogr. 2006 Apr;62(Pt 4):433-8. | ||||
| REF 10 | 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. | ||||
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