eF-site ID 4xbf-ABD PDB Code 4xbf Chain A, B, D click to enlarge Title Structure of LSD1:CoREST in complex with ssRNA Classification Oxidoreductase/Transcription/RNA Compound Lysine-specific histone demethylase 1A Source Homo sapiens (Human) (4XBF) Sequence A:  PSGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVF LFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSDTVLVH RVHSYLERHGLINFGIYKRIKPLPTKKTGKVIIIGSGVSG LAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLG AMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAV PKEKDEMVEQEFNRLLEATSYLSHQLDFNVLNNKPVSLGQ ALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVN LKEKIKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTAL CKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDRQILD WHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNG YSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRST SQTFIYKCDAVLCTLPLGVLKQQPPAVQFVPPLPEWKTSA VQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGE LFLFWNLYKAPILLALVAGEAAGIMENISDDVIVGRCLAI LKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSG NDYDLMAQPITPGPSIPGAPQPIPRLFFAGEHTIRNYPAT VHGALLSGLREAGRIADQFLGAMYTL B:  RKPPKGMFLSQEDVEAVSANATAATTVLRQLDMELVSVKR QIQNIKQTNSALKEKLDGGIEPYRLPEVIQKCNARWTTEE QLLAVQAIRKYGRDFQAISDVIGNKSVVQVKNFFVNYRRR FNIDEVLQEWEAE D:  UUAGG Description Functional site 1) chain A residue 285 type sequence G description binding site for residue FAD A 901 source : AC1 2) chain A residue 287 type sequence G description binding site for residue FAD A 901 source : AC1 3) chain A residue 288 type sequence V description binding site for residue FAD A 901 source : AC1 4) chain A residue 289 type sequence S description binding site for residue FAD A 901 source : AC1 5) chain A residue 308 type sequence E description binding site for residue FAD A 901 source : AC1 6) chain A residue 309 type sequence A description binding site for residue FAD A 901 source : AC1 7) chain A residue 310 type sequence R description binding site for residue FAD A 901 source : AC1 8) chain A residue 314 type sequence G description binding site for residue FAD A 901 source : AC1 9) chain A residue 315 type sequence G description binding site for residue FAD A 901 source : AC1 10) chain A residue 316 type sequence R description binding site for residue FAD A 901 source : AC1 11) chain A residue 317 type sequence V description binding site for residue FAD A 901 source : AC1 12) chain A residue 329 type sequence L description binding site for residue FAD A 901 source : AC1 13) chain A residue 330 type sequence G description binding site for residue FAD A 901 source : AC1 14) chain A residue 331 type sequence A description binding site for residue FAD A 901 source : AC1 15) chain A residue 332 type sequence M description binding site for residue FAD A 901 source : AC1 16) chain A residue 333 type sequence V description binding site for residue FAD A 901 source : AC1 17) chain A residue 588 type sequence T description binding site for residue FAD A 901 source : AC1 18) chain A residue 590 type sequence V description binding site for residue FAD A 901 source : AC1 19) chain A residue 624 type sequence T description binding site for residue FAD A 901 source : AC1 20) chain A residue 625 type sequence L description binding site for residue FAD A 901 source : AC1 21) chain A residue 626 type sequence P description binding site for residue FAD A 901 source : AC1 22) chain A residue 637 type sequence V description binding site for residue FAD A 901 source : AC1 23) chain A residue 751 type sequence W description binding site for residue FAD A 901 source : AC1 24) chain A residue 756 type sequence W description binding site for residue FAD A 901 source : AC1 25) chain A residue 760 type sequence S description binding site for residue FAD A 901 source : AC1 26) chain A residue 761 type sequence Y description binding site for residue FAD A 901 source : AC1 27) chain A residue 800 type sequence G description binding site for residue FAD A 901 source : AC1 28) chain A residue 801 type sequence E description binding site for residue FAD A 901 source : AC1 29) chain A residue 810 type sequence T description binding site for residue FAD A 901 source : AC1 30) chain A residue 811 type sequence V description binding site for residue FAD A 901 source : AC1 31) chain A residue 814 type sequence A description binding site for residue FAD A 901 source : AC1 32) chain A residue 751 type sequence W description binding site for residue SO4 A 902 source : AC2 33) chain A residue 754 type sequence D description binding site for residue SO4 A 902 source : AC2 34) chain A residue 310 type sequence R description binding site for residue SO4 A 903 source : AC3 35) chain A residue 312 type sequence R description binding site for residue SO4 A 903 source : AC3 36) chain A residue 374 type sequence K description binding site for residue SO4 A 904 source : AC4 37) chain A residue 522 type sequence S description binding site for residue SO4 A 904 source : AC4 38) chain A residue 524 type sequence R description binding site for residue SO4 A 904 source : AC4 39) chain A residue 687 type sequence S description binding site for residue SO4 A 905 source : AC5 40) chain A residue 690 type sequence E description binding site for residue SO4 A 905 source : AC5 41) chain B residue 389 type sequence L description binding site for residue SO4 A 905 source : AC5 42) chain A residue 189 type sequence T description binding site for residue SO4 A 906 source : AC6 43) chain A residue 190 type sequence S description binding site for residue SO4 A 906 source : AC6 44) chain A residue 409 type sequence G description binding site for residue GOL A 907 source : AC7 45) chain A residue 413 type sequence E description binding site for residue GOL A 907 source : AC7 46) chain A residue 526 type sequence R description binding site for residue GOL A 907 source : AC7 47) chain A residue 533 type sequence F description binding site for residue GOL A 907 source : AC7 48) chain A residue 688 type sequence R description binding site for residue GOL A 907 source : AC7 49) chain A residue 289 type BINDING sequence S description BINDING => ECO:0000269|PubMed:16885027, ECO:0000269|PubMed:16956976, ECO:0000269|PubMed:21300290, ECO:0000269|PubMed:23721412, ECO:0007744|PDB:2DW4, ECO:0007744|PDB:2H94, ECO:0007744|PDB:2HKO, ECO:0007744|PDB:2IW5, ECO:0007744|PDB:2V1D, ECO:0007744|PDB:2X0L, ECO:0007744|PDB:2XAF, ECO:0007744|PDB:2XAG, ECO:0007744|PDB:2XAH, ECO:0007744|PDB:2XAJ, ECO:0007744|PDB:2XAQ, ECO:0007744|PDB:2XAS, ECO:0007744|PDB:2Y48, ECO:0007744|PDB:3ZMS, ECO:0007744|PDB:3ZMT, ECO:0007744|PDB:3ZMU, ECO:0007744|PDB:3ZMV, ECO:0007744|PDB:3ZMZ, ECO:0007744|PDB:3ZN0, ECO:0007744|PDB:3ZN1 source Swiss-Prot : SWS_FT_FI1 50) chain A residue 308 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16885027, ECO:0000269|PubMed:16956976, ECO:0000269|PubMed:21300290, ECO:0000269|PubMed:23721412, ECO:0007744|PDB:2DW4, ECO:0007744|PDB:2H94, ECO:0007744|PDB:2HKO, ECO:0007744|PDB:2IW5, ECO:0007744|PDB:2V1D, ECO:0007744|PDB:2X0L, ECO:0007744|PDB:2XAF, ECO:0007744|PDB:2XAG, ECO:0007744|PDB:2XAH, ECO:0007744|PDB:2XAJ, ECO:0007744|PDB:2XAQ, ECO:0007744|PDB:2XAS, ECO:0007744|PDB:2Y48, ECO:0007744|PDB:3ZMS, ECO:0007744|PDB:3ZMT, ECO:0007744|PDB:3ZMU, ECO:0007744|PDB:3ZMV, ECO:0007744|PDB:3ZMZ, ECO:0007744|PDB:3ZN0, ECO:0007744|PDB:3ZN1 source Swiss-Prot : SWS_FT_FI1 51) chain A residue 310 type BINDING sequence R description BINDING => ECO:0000269|PubMed:16885027, ECO:0000269|PubMed:16956976, ECO:0000269|PubMed:21300290, ECO:0000269|PubMed:23721412, ECO:0007744|PDB:2DW4, ECO:0007744|PDB:2H94, ECO:0007744|PDB:2HKO, ECO:0007744|PDB:2IW5, ECO:0007744|PDB:2V1D, ECO:0007744|PDB:2X0L, ECO:0007744|PDB:2XAF, ECO:0007744|PDB:2XAG, ECO:0007744|PDB:2XAH, ECO:0007744|PDB:2XAJ, ECO:0007744|PDB:2XAQ, ECO:0007744|PDB:2XAS, ECO:0007744|PDB:2Y48, ECO:0007744|PDB:3ZMS, ECO:0007744|PDB:3ZMT, ECO:0007744|PDB:3ZMU, ECO:0007744|PDB:3ZMV, ECO:0007744|PDB:3ZMZ, ECO:0007744|PDB:3ZN0, ECO:0007744|PDB:3ZN1 source Swiss-Prot : SWS_FT_FI1 52) chain A residue 316 type BINDING sequence R description BINDING => ECO:0000269|PubMed:16885027, ECO:0000269|PubMed:16956976, ECO:0000269|PubMed:21300290, ECO:0000269|PubMed:23721412, ECO:0007744|PDB:2DW4, ECO:0007744|PDB:2H94, ECO:0007744|PDB:2HKO, ECO:0007744|PDB:2IW5, ECO:0007744|PDB:2V1D, ECO:0007744|PDB:2X0L, ECO:0007744|PDB:2XAF, ECO:0007744|PDB:2XAG, ECO:0007744|PDB:2XAH, ECO:0007744|PDB:2XAJ, ECO:0007744|PDB:2XAQ, ECO:0007744|PDB:2XAS, ECO:0007744|PDB:2Y48, ECO:0007744|PDB:3ZMS, ECO:0007744|PDB:3ZMT, ECO:0007744|PDB:3ZMU, ECO:0007744|PDB:3ZMV, ECO:0007744|PDB:3ZMZ, ECO:0007744|PDB:3ZN0, ECO:0007744|PDB:3ZN1 source Swiss-Prot : SWS_FT_FI1 53) chain A residue 332 type BINDING sequence M description BINDING => ECO:0000269|PubMed:16885027, ECO:0000269|PubMed:16956976, ECO:0000269|PubMed:21300290, ECO:0000269|PubMed:23721412, ECO:0007744|PDB:2DW4, ECO:0007744|PDB:2H94, ECO:0007744|PDB:2HKO, ECO:0007744|PDB:2IW5, ECO:0007744|PDB:2V1D, ECO:0007744|PDB:2X0L, ECO:0007744|PDB:2XAF, ECO:0007744|PDB:2XAG, ECO:0007744|PDB:2XAH, ECO:0007744|PDB:2XAJ, ECO:0007744|PDB:2XAQ, ECO:0007744|PDB:2XAS, ECO:0007744|PDB:2Y48, ECO:0007744|PDB:3ZMS, ECO:0007744|PDB:3ZMT, ECO:0007744|PDB:3ZMU, ECO:0007744|PDB:3ZMV, ECO:0007744|PDB:3ZMZ, ECO:0007744|PDB:3ZN0, ECO:0007744|PDB:3ZN1 source Swiss-Prot : SWS_FT_FI1 54) chain A residue 801 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16885027, ECO:0000269|PubMed:16956976, ECO:0000269|PubMed:21300290, ECO:0000269|PubMed:23721412, ECO:0007744|PDB:2DW4, ECO:0007744|PDB:2H94, ECO:0007744|PDB:2HKO, ECO:0007744|PDB:2IW5, ECO:0007744|PDB:2V1D, ECO:0007744|PDB:2X0L, ECO:0007744|PDB:2XAF, ECO:0007744|PDB:2XAG, ECO:0007744|PDB:2XAH, ECO:0007744|PDB:2XAJ, ECO:0007744|PDB:2XAQ, ECO:0007744|PDB:2XAS, ECO:0007744|PDB:2Y48, ECO:0007744|PDB:3ZMS, ECO:0007744|PDB:3ZMT, ECO:0007744|PDB:3ZMU, ECO:0007744|PDB:3ZMV, ECO:0007744|PDB:3ZMZ, ECO:0007744|PDB:3ZN0, ECO:0007744|PDB:3ZN1 source Swiss-Prot : SWS_FT_FI1 55) chain A residue 810 type BINDING sequence T description BINDING => ECO:0000269|PubMed:16885027, ECO:0000269|PubMed:16956976, ECO:0000269|PubMed:21300290, ECO:0000269|PubMed:23721412, ECO:0007744|PDB:2DW4, ECO:0007744|PDB:2H94, ECO:0007744|PDB:2HKO, ECO:0007744|PDB:2IW5, ECO:0007744|PDB:2V1D, ECO:0007744|PDB:2X0L, ECO:0007744|PDB:2XAF, ECO:0007744|PDB:2XAG, ECO:0007744|PDB:2XAH, ECO:0007744|PDB:2XAJ, ECO:0007744|PDB:2XAQ, ECO:0007744|PDB:2XAS, ECO:0007744|PDB:2Y48, ECO:0007744|PDB:3ZMS, ECO:0007744|PDB:3ZMT, ECO:0007744|PDB:3ZMU, ECO:0007744|PDB:3ZMV, ECO:0007744|PDB:3ZMZ, ECO:0007744|PDB:3ZN0, ECO:0007744|PDB:3ZN1 source Swiss-Prot : SWS_FT_FI1 56) chain A residue 611 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 57) chain A residue 442 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI3 58) chain A residue 469 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI3 59) chain A residue 503 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:25018020 source Swiss-Prot : SWS_FT_FI4

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