eF-site ID 1efc-AB PDB Code 1efc Chain A, B click to enlarge Title INTACT ELONGATION FACTOR FROM E.COLI Classification RNA BINDING PROTEIN Compound PROTEIN (ELONGATION FACTOR) Source (EFTU_ECOLI) Sequence A:  TKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFD QIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADY VKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGV PYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDT PIVRGSALKALEGDAEWEAKILELAGFLDSYIPEPERAID KPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGI KETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIE RGQVLAKPGTIKPHTKFESEVYILSKDEGGRHTPFFKGYR PQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIA MDDGLRFAIREGGRTVGAGVVAKVLS B:  TKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFD QIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADY VKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGV PYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDT PIVRGSALKALEGDAEWEAKILELAGFLDSYIPEPERAID KPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGI KETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIE RGQVLAKPGTIKPHTKFESEVYILSKDEGGRHTPFFKGYR PQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIA MDDGLRFAIREGGRTVGAGVVAKVLS Description Functional site 1) chain A residue 25 type sequence T description BINDING SITE FOR RESIDUE MG A 501 source : AC1 2) chain B residue 25 type sequence T description BINDING SITE FOR RESIDUE MG B 502 source : AC2 3) chain A residue 21 type sequence D description BINDING SITE FOR RESIDUE GDP A 513 source : AC3 4) chain A residue 22 type sequence H description BINDING SITE FOR RESIDUE GDP A 513 source : AC3 5) chain A residue 23 type sequence G description BINDING SITE FOR RESIDUE GDP A 513 source : AC3 6) chain A residue 24 type sequence K description BINDING SITE FOR RESIDUE GDP A 513 source : AC3 7) chain A residue 25 type sequence T description BINDING SITE FOR RESIDUE GDP A 513 source : AC3 8) chain A residue 26 type sequence T description BINDING SITE FOR RESIDUE GDP A 513 source : AC3 9) chain A residue 46 type sequence F description BINDING SITE FOR RESIDUE GDP A 513 source : AC3 10) chain A residue 135 type sequence N description BINDING SITE FOR RESIDUE GDP A 513 source : AC3 11) chain A residue 136 type sequence K description BINDING SITE FOR RESIDUE GDP A 513 source : AC3 12) chain A residue 138 type sequence D description BINDING SITE FOR RESIDUE GDP A 513 source : AC3 13) chain A residue 139 type sequence M description BINDING SITE FOR RESIDUE GDP A 513 source : AC3 14) chain A residue 173 type sequence S description BINDING SITE FOR RESIDUE GDP A 513 source : AC3 15) chain A residue 174 type sequence A description BINDING SITE FOR RESIDUE GDP A 513 source : AC3 16) chain A residue 175 type sequence L description BINDING SITE FOR RESIDUE GDP A 513 source : AC3 17) chain B residue 21 type sequence D description BINDING SITE FOR RESIDUE GDP B 514 source : AC4 18) chain B residue 22 type sequence H description BINDING SITE FOR RESIDUE GDP B 514 source : AC4 19) chain B residue 23 type sequence G description BINDING SITE FOR RESIDUE GDP B 514 source : AC4 20) chain B residue 24 type sequence K description BINDING SITE FOR RESIDUE GDP B 514 source : AC4 21) chain B residue 25 type sequence T description BINDING SITE FOR RESIDUE GDP B 514 source : AC4 22) chain B residue 26 type sequence T description BINDING SITE FOR RESIDUE GDP B 514 source : AC4 23) chain B residue 46 type sequence F description BINDING SITE FOR RESIDUE GDP B 514 source : AC4 24) chain B residue 135 type sequence N description BINDING SITE FOR RESIDUE GDP B 514 source : AC4 25) chain B residue 136 type sequence K description BINDING SITE FOR RESIDUE GDP B 514 source : AC4 26) chain B residue 138 type sequence D description BINDING SITE FOR RESIDUE GDP B 514 source : AC4 27) chain B residue 139 type sequence M description BINDING SITE FOR RESIDUE GDP B 514 source : AC4 28) chain B residue 173 type sequence S description BINDING SITE FOR RESIDUE GDP B 514 source : AC4 29) chain B residue 174 type sequence A description BINDING SITE FOR RESIDUE GDP B 514 source : AC4 30) chain B residue 175 type sequence L description BINDING SITE FOR RESIDUE GDP B 514 source : AC4 31) chain A residue 18 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI1 32) chain A residue 80 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 33) chain A residue 135 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI1 34) chain B residue 18 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI1 35) chain B residue 80 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 36) chain B residue 135 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI1 37) chain A residue 37 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI3 38) chain B residue 294 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI3 39) chain A residue 176 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI3 40) chain A residue 248 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI3 41) chain A residue 252 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI3 42) chain A residue 294 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI3 43) chain B residue 37 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI3 44) chain B residue 176 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI3 45) chain B residue 248 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI3 46) chain B residue 252 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI3 47) chain A residue 56 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_FI4 48) chain B residue 56 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_FI4 49) chain A residue 313 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI5 50) chain B residue 313 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI5 51) chain A residue 50-65 type prosite sequence DNAPEEKARGITINTS description G_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DNapeEKaRGITIntS source prosite : PS00301 52) chain A residue 21 type catalytic sequence D description 535 source MCSA : MCSA1 53) chain A residue 24 type catalytic sequence K description 535 source MCSA : MCSA1 54) chain A residue 25 type catalytic sequence T description 535 source MCSA : MCSA1 55) chain A residue 84 type catalytic sequence H description 535 source MCSA : MCSA1 56) chain B residue 21 type catalytic sequence D description 535 source MCSA : MCSA2 57) chain B residue 24 type catalytic sequence K description 535 source MCSA : MCSA2 58) chain B residue 25 type catalytic sequence T description 535 source MCSA : MCSA2 59) chain B residue 84 type catalytic sequence H description 535 source MCSA : MCSA2 60) chain A residue 382 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:19150849, ECO:0000269|PubMed:24141193, ECO:0000269|PubMed:8416965 source Swiss-Prot : SWS_FT_FI6 61) chain B residue 382 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:19150849, ECO:0000269|PubMed:24141193, ECO:0000269|PubMed:8416965 source Swiss-Prot : SWS_FT_FI6

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