eF-site ID 6qk7-ABCD PDB Code 6qk7 Chain A, B, C, D click to enlarge Title Elongator catalytic subcomplex Elp123 lobe Classification TRANSLATION Compound Elongator complex protein 1 Source ORGANISM_COMMON: Baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae (strain ATCC 204508 / S288c); Sequence A:  MRNLITLNKGKFKPTASTAEGDEDDLSFTLLDSVFDTLSD SITCVLGSTDIGAIEVQQFMKDGSRNVLASFNIQTFDDKL LSFVHFADINQLVFVFEQGDIITATYDPVSLDPAETLIEI MGTIDNGIAAAQWSYDEETLAMVTKDRNVVVLSKLFEPIS EYHLEVDTGDVTALDSHEITISWRGDCDYFAVSSVEEVIK RRAFRVFSREGQLDSASEPVTGMEHQLSWKPQGSLIASIQ RKTDLGEEDSVDVIFFERNGLRHGEFDTRLPLDEKVESVC WNSNSEALAVVLANRIQLWTSKNYHWYLKQELYASDISYV KWHPEKDFTLMFSDAGFINIVDFAYKMAQGPTLEPFDNGT SLVVDGRTVNITPLALANVPPPMYYRDFETPGNVLDVACS FSNEIYAAINKDVLIFAAVPSIEEMKKGKHPSIVCEFPKS EFTSEVDSLRQVAFINDSIVGVLLDTDNLSRIALLDIQDI TQPTLITIVEVYDKIVLLRSDFDYNHLVYETRDGTVCQLD AEGQLMEITKFPQLVRDFRVKRVHNTSAEDDDNWSAESSE LVAFGITNNGKLFANQVLLASAVTSLEITDSFLLFTTAQH NLQFVHLNSTDFKPLPLVEEGVEDERVRAIERGSILVSVI PSKSSVVLQATRGNLETIYPRIMVLAEVRKNIMAKRYKEA FIVCRTHRINLDILHDYAPELFIENLEVFINQIGRVDYLN LFISCLSEDDVTKTKYKETLYSGISKSFGMEPAPLTEMQI YMKKKMFDPKTSKVNKICDAVLNVLLSNPEYKKKYLQTII TAYASQNPQNLSAALKLISELENSEEKDSCVTYLCFLQDV NVVYKSALSLYDVSLALLVAQKSQMDPREYLPFLQELQDN EPLRRKFLIDDYLGNYEKALEHLSEIDKDGNVSEEVIDYV ESHDLYKHGLALYRYDSEKQNVIYNIYAKHLSSNQMYTDA AVAYEMLGKLKEAMGAYQSAKRWREAMSIAVQKFPEEVES VAEELISSLTFEHRYVDAADIQLEYLDNVKEAVALYCKAY RYDIASLVAIKAKKDELLEEVVDPGLGEGFGIIAELLADC KGQINSQLRRLREEYLVQSVGRLIERLNQTKPDAVRVVEG LCRRNMREQAHQIQKNFVEVLDLLKANVEIHDFPKSHIVD F B:  ECITPEAIFIGANKQTQVSDIHKVKKIVAFGAGKTIALWD PIEPNNKGVYATLKGHEAEVTCVRFVPDSDFMVSASEDHH VKIWKFTDYSHLQCIQTIQHYSKTIVALSALPSLISVGCA DGTISIWRQNIQNDEFGLAHEFTIKKGFFYPLCLSLSKVE EKKYLLAIGGTNVNVFIASFILSDSGIEKCRVVAELEGHE DWVKSLAFRHQETPGDYLLCSGSQDRYIRLWRIRINDLID DSEEDSKKLTLLSNKQYKFQIDDELRVGINFEALIMGHDD WISSLQWHESRLQLLAATADTSLMVWEPDETSGIWVCSLR LGESGGFWSCLWFTHERMDFFLTNGKTGSWRMWATKDNII CDQRLGISGATKDVTDIAWSPSGEYLLATSLDQTTRLFAP WIYDASGRKREIATWHEFSRPQIHGYDMICVETVTDTRFV SGGDEKILRSFDLPKGVAGMLQKFVGIQFEEKSEMPDSAT VPVLGLSNKAGSLLECPPMEDQLQRHLLWPEVEKLYGHGF EITCLDISPDQKLIASACRSNNVQNAVIRIFSTENWLEIK PALPFHSLTITRLKFSKDGKFLLSVCRDRKWALWERNMED NTFELRFKNEKPHTRIIWDADWAPLEFGNVFVTASRDKTV KVWRHQKEPADDYVLEASIKHTKAVTAISIHDSMIREKIL ISVGLENGEIYLYSYTLGKFELITQLNEDITPADKITRLR WSHLKRNGKLFLGVGSSDLSTRIYSLAYE C:  SGIAVVAVMCKPHRCPHIAYTGNICVYCPGGPDSDFEYST QSYTGYEPTSMRAIRARYDPYEQARGRVEQLKQLGHSIDK VEYVLMGGTFMSLPKEYREDFIVKLHNALSGFNGNDIDEA ILYSQQSLTKCVGITIETRPDYCTQTHLDDMLKYGCTRLE IGVQSLYEDVARDTNRGHTVRSVCETFAVSKDAGYKVVSH MMPDLPNVGMERDIEQFKEYFENPDFRTDGLKIYPTLVIR GTGLYELWKTGRYKSYSANALVDLVARILALVPPWTRIYR VQRDIPMPLVTSGVDNGNLRELALARMKDLGTTCRDVRTR EVGVQPDQVELIRRDYYANGGWETFLSYEDPKKDILIGLL RLRKASKKYTYRKEFTSQRTSIVRELHVYGQHQGFGTLLM EEAERIAKEEHGSEKISVISGVGVRNYYGKLGYELDGPYM SKRI D:  LYKHGLALYRYDSEKQNVIYNIYAKHLSSNQMYTDAAVAY EMLGKLKEAMGAYQSAKRWREAMSIAVQKFPEEVESVAEE LISSLTFEHRYVDAADIQLEYLDNVKEAVALYCKAYRYDI ASLVAIKAKKDELLEEVVDPGLGEGFGIIAELLADCKGQI NSQLRREEYLVQSVGRLIERLNQTKPDAVRVVEGLCRRNM REQAHQIQKNFVEVLDLLKANVKEIEIHDFPKSHIVDF Description (1)  Elongator complex protein 1, Elongator complex protein 2, Elongator complex protein 3 (E.C.2.3.1.48) Functional site 1) chain C residue 108 type sequence C description binding site for residue SF4 C 601 source : AC1 2) chain C residue 110 type sequence H description binding site for residue SF4 C 601 source : AC1 3) chain C residue 118 type sequence C description binding site for residue SF4 C 601 source : AC1 4) chain C residue 121 type sequence C description binding site for residue SF4 C 601 source : AC1 5) chain C residue 269 type sequence R description binding site for residue SF4 C 601 source : AC1 6) chain C residue 120 type sequence Y description binding site for residue 5AD C 602 source : AC2 7) chain C residue 257 type sequence Q description binding site for residue 5AD C 602 source : AC2 8) chain C residue 293 type sequence H description binding site for residue 5AD C 602 source : AC2 9) chain C residue 295 type sequence M description binding site for residue 5AD C 602 source : AC2 10) chain C residue 327 type sequence Y description binding site for residue 5AD C 602 source : AC2 11) chain C residue 328 type sequence P description binding site for residue 5AD C 602 source : AC2 12) chain C residue 330 type sequence L description binding site for residue 5AD C 602 source : AC2 13) chain C residue 376 type sequence R description binding site for residue 5AD C 602 source : AC2 14) chain C residue 108 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16420352, ECO:0000269|PubMed:31309145, ECO:0007744|PDB:6QK7 source Swiss-Prot : SWS_FT_FI1 15) chain C residue 118 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16420352, ECO:0000269|PubMed:31309145, ECO:0007744|PDB:6QK7 source Swiss-Prot : SWS_FT_FI1 16) chain C residue 121 type BINDING sequence C description BINDING => ECO:0000269|PubMed:16420352, ECO:0000269|PubMed:31309145, ECO:0007744|PDB:6QK7 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 636 type BINDING sequence S description BINDING => ECO:0000269|PubMed:16420352, ECO:0000269|PubMed:31309145, ECO:0007744|PDB:6QK7 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 828 type BINDING sequence S description BINDING => ECO:0000269|PubMed:16420352, ECO:0000269|PubMed:31309145, ECO:0007744|PDB:6QK7 source Swiss-Prot : SWS_FT_FI1 19) chain C residue 453 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:12872131 source Swiss-Prot : SWS_FT_FI3 20) chain C residue 173 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:A0A1C7D1B7 source Swiss-Prot : SWS_FT_FI2 21) chain C residue 485 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:A0A1C7D1B7 source Swiss-Prot : SWS_FT_FI2 22) chain C residue 508 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:A0A1C7D1B7 source Swiss-Prot : SWS_FT_FI2 23) chain C residue 541 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:A0A1C7D1B7 source Swiss-Prot : SWS_FT_FI2

Display surface Download Links