eF-site ID 5o8w-AB PDB Code 5o8w Chain A, B click to enlarge Title CRYSTAL STRUCTURE ANALYSIS OF THE YEAST ELONGATION FACTOR COMPLEX EEF1A:EEF1BA Classification TRANSLATION Compound Elongation factor 1-alpha Source (EF1B_YEAST) Sequence A:  GKEKSHINVVVIGHVDSGKSTTTGHLIYXCGGIDKRTIEK FEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWXFE TPKYQVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGVG EFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDSVKWD ESRFQEIVKETSNFIKKVGYNPKTVPFVPISGWNGDNMIE ATTNAPWYKGWEKETKAGVVKGKTLLEAIDAIEQPSRPTD KPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFAPA GVTTEVKSVEMHHEQLEQGVPGDNVGFNVKNVSVKEIRRG NVCGDAKNDPPKGCASFNATVIVLNHPGQISAGYSPVLDC HTAHIACRFDELLEKNDRRSGKKLEDHPKFLKSGDAALVK FVPSKPMCVEAFSEYPPLGRFAVRDMRQTVAVGVIKSVDK TXXXXXXXX B:  PAKPAAKSIVTLDVKPWDDETNLEEXVANVKAIEXEGLTW GAHQFIPIGFGIKKLQINCVVEDDKVSLDDLQQSIEEDED HVQSTDIAAXQKL Description (1)  Elongation factor 1-alpha, Elongation factor 1-beta Functional site 1) chain A residue 45 type sequence E description binding site for residue GLN A 501 source : AC1 2) chain A residue 48 type sequence E description binding site for residue GLN A 501 source : AC1 3) chain A residue 339 type sequence N description binding site for residue GLN A 501 source : AC1 4) chain A residue 374 type sequence L description binding site for residue GLN A 501 source : AC1 5) chain A residue 273 type sequence G description binding site for residue PGE A 502 source : AC2 6) chain A residue 286 type sequence E description binding site for residue PGE A 502 source : AC2 7) chain A residue 385 type sequence L description binding site for residue PGE A 502 source : AC2 8) chain A residue 386 type sequence E description binding site for residue PGE A 502 source : AC2 9) chain A residue 384 type sequence K description binding site for residue PGE A 503 source : AC3 10) chain A residue 385 type sequence L description binding site for residue PGE A 503 source : AC3 11) chain A residue 387 type sequence D description binding site for residue PGE A 503 source : AC3 12) chain A residue 96 type sequence R description binding site for residue PGE B 1301 source : AC4 13) chain A residue 428 type sequence R description binding site for residue PGE B 1301 source : AC4 14) chain B residue 1176 type sequence D description binding site for residue PGE B 1301 source : AC4 15) chain B residue 1177 type sequence D description binding site for residue PGE B 1301 source : AC4 16) chain B residue 1178 type sequence K description binding site for residue PGE B 1301 source : AC4 17) chain B residue 1179 type sequence V description binding site for residue PGE B 1301 source : AC4 18) chain B residue 1180 type sequence S description binding site for residue PGE B 1301 source : AC4 19) chain A residue 414 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI13 20) chain A residue 224 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI15 21) chain A residue 242 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI15 22) chain A residue 253 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI15 23) chain A residue 271 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI15 24) chain A residue 393 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI15 25) chain A residue 437 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI15 26) chain A residue 61-76 type prosite sequence DKLKAERERGITIDIA description G_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DKlkaEReRGITIdiA source prosite : PS00301 27) chain B residue 1195-1206 type prosite sequence VQSTDIAAXQKL description EF1BD_2 Elongation factor 1 beta/beta'/delta chain signature 2. VQStDIaAMQKL source prosite : PS00825 28) chain A residue 14 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI1 29) chain A residue 91 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 30) chain A residue 153 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI1 31) chain A residue 298 type SITE sequence E description Not modified source Swiss-Prot : SWS_FT_FI2 32) chain A residue 372 type SITE sequence E description Not modified source Swiss-Prot : SWS_FT_FI2 33) chain A residue 2 type MOD_RES sequence G description N,N,N-trimethylglycine; by EFM7 => ECO:0000269|PubMed:26545399 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 3 type MOD_RES sequence K description N6-methyllysine; by EFM7; alternate => ECO:0000269|PubMed:26545399 source Swiss-Prot : SWS_FT_FI4 35) chain A residue 18 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17287358 source Swiss-Prot : SWS_FT_FI5 36) chain A residue 163 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17287358 source Swiss-Prot : SWS_FT_FI5 37) chain A residue 30 type MOD_RES sequence X description N6-methyllysine; by EFM1 => ECO:0000269|PubMed:22522802, ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:8476932 source Swiss-Prot : SWS_FT_FI6 38) chain A residue 72 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17287358 source Swiss-Prot : SWS_FT_FI7 39) chain A residue 82 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17287358 source Swiss-Prot : SWS_FT_FI7 40) chain A residue 430 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17287358 source Swiss-Prot : SWS_FT_FI7 41) chain A residue 79 type MOD_RES sequence X description N6,N6,N6-trimethyllysine; by EFM5 => ECO:0000269|PubMed:22522802, ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:25446118, ECO:0000269|PubMed:8476932 source Swiss-Prot : SWS_FT_FI8 42) chain A residue 259 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI9 43) chain A residue 289 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI10 44) chain A residue 316 type MOD_RES sequence K description N6-methyllysine; by EFM4; alternate => ECO:0000269|PubMed:24517342 source Swiss-Prot : SWS_FT_FI11 45) chain A residue 390 type MOD_RES sequence K description N6-methyllysine; by EFM6 => ECO:0000269|PubMed:22522802, ECO:0000269|PubMed:24517342, ECO:0000269|PubMed:26115316, ECO:0000269|PubMed:8476932 source Swiss-Prot : SWS_FT_FI12

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