eF-site ID 5mi9-A PDB Code 5mi9 Chain A click to enlarge Title Structure of the phosphomimetic mutant of the elongation factor EF-Tu T62E Classification HYDROLASE Compound Elongation factor Tu 1 Source (EFTU1_ECOHS) Sequence A:  TKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFD QIDNAPEEKARGIEINTSHVEYDTPTRHYAHVDCPGHADY VKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGV PYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDT PIVRGSALKALEGDAEWEAKILELAGFLDSYIPEPERAID KPFLLPIEDVFSICGRGTVVTGRVERGIIKVGEEVEIVGI KETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIE RGQVLAKPGTIKPHTKFESEVYILSKDEGGRHTPFFKGYR PQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIA MDDGLRFAIREGGRTVGAGVVAKVL Description Functional site 1) chain A residue 26 type sequence T description binding site for residue MG A 401 source : AC1 2) chain A residue 20 type sequence H description binding site for residue GDP A 402 source : AC2 3) chain A residue 22 type sequence D description binding site for residue GDP A 402 source : AC2 4) chain A residue 23 type sequence H description binding site for residue GDP A 402 source : AC2 5) chain A residue 24 type sequence G description binding site for residue GDP A 402 source : AC2 6) chain A residue 25 type sequence K description binding site for residue GDP A 402 source : AC2 7) chain A residue 26 type sequence T description binding site for residue GDP A 402 source : AC2 8) chain A residue 27 type sequence T description binding site for residue GDP A 402 source : AC2 9) chain A residue 47 type sequence F description binding site for residue GDP A 402 source : AC2 10) chain A residue 137 type sequence K description binding site for residue GDP A 402 source : AC2 11) chain A residue 174 type sequence S description binding site for residue GDP A 402 source : AC2 12) chain A residue 175 type sequence A description binding site for residue GDP A 402 source : AC2 13) chain A residue 176 type sequence L description binding site for residue GDP A 402 source : AC2 14) chain A residue 22 type catalytic sequence D description 535 source MCSA : MCSA1 15) chain A residue 25 type catalytic sequence K description 535 source MCSA : MCSA1 16) chain A residue 26 type catalytic sequence T description 535 source MCSA : MCSA1 17) chain A residue 85 type catalytic sequence H description 535 source MCSA : MCSA1 18) chain A residue 19 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI1 19) chain A residue 81 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 20) chain A residue 136 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI1 21) chain A residue 57 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:2022614, ECO:0000269|PubMed:389663, ECO:0000269|PubMed:6997043, ECO:0000269|PubMed:7021545 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 314 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI4 23) chain A residue 383 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:19150849, ECO:0000269|PubMed:24141193, ECO:0000269|PubMed:8416965 source Swiss-Prot : SWS_FT_FI5

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