eF-site ID 2x0l-ABC PDB Code 2x0l Chain A, B, C click to enlarge Title Crystal structure of a neuro-specific splicing variant of human histone lysine demethylase LSD1. Classification TRANSCRIPTION Compound LYSINE-SPECIFIC HISTONE DEMETHYLASE 1 Source null (Q5TEC6_HUMAN) Sequence A:  PSGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVF LFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSDTVLVH RVHSYLERHGLINFGIYKRIKPLPTKKTGKVIIIGSGVSG LAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLG AMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAD TVKVPKEKDEMVEQEFNRLLEATSYLSHQLDFNVLNNKPV SLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLN KMVNLKEKIKELHQQYKEASEVKPPRDITAEFLVKSKHRD LTALCKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDR QILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLT VRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVN TRSTSQTFIYKCDAVLCTLPLGVLKQQPPAVQFVPPLPEW KTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTA SRGELFLFWNLYKAPILLALVAGEAAGIMENISDDVIVGR CLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAA GSSGNDYDLMAQPITPGPSIPGAPQPIPRLFFAGEHTIRN YPATVHGALLSGLREAGRIADQFLGAMYTL B:  RKPPKGMFLSQEDVEAVSANATAATTVLRQLDMELVSVKR QIQNIKQTNSALKEKLDGGIEPYRLPEVIQKCNARWTTEE QLLAVQAIRKYGRDFQAISDVIGNKSVVQVKNFFVNYRRR FNIDEVLQEWEAE C:  ARTMQTARKSTGGKAP Description Functional site 1) chain A residue 285 type sequence G description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 2) chain A residue 287 type sequence G description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 3) chain A residue 288 type sequence V description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 4) chain A residue 289 type sequence S description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 5) chain A residue 307 type sequence L description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 6) chain A residue 308 type sequence E description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 7) chain A residue 309 type sequence A description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 8) chain A residue 310 type sequence R description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 9) chain A residue 314 type sequence G description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 10) chain A residue 315 type sequence G description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 11) chain A residue 316 type sequence R description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 12) chain A residue 329 type sequence L description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 13) chain A residue 330 type sequence G description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 14) chain A residue 331 type sequence A description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 15) chain A residue 332 type sequence M description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 16) chain A residue 333 type sequence V description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 17) chain A residue 588 type sequence T description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 18) chain A residue 590 type sequence V description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 19) chain A residue 624 type sequence T description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 20) chain A residue 625 type sequence L description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 21) chain A residue 626 type sequence P description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 22) chain A residue 756 type sequence W description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 23) chain A residue 760 type sequence S description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 24) chain A residue 761 type sequence Y description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 25) chain A residue 800 type sequence G description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 26) chain A residue 801 type sequence E description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 27) chain A residue 809 type sequence A description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 28) chain A residue 810 type sequence T description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 29) chain A residue 811 type sequence V description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 30) chain C residue 4 type sequence M description BINDING SITE FOR RESIDUE FAD A 900 source : AC1 31) chain C residue 9 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI7 32) chain C residue 10 type MOD_RES sequence S description Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16457588 source Swiss-Prot : SWS_FT_FI8 33) chain C residue 14 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI10 34) chain A residue 503 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI10 35) chain C residue 2 type MOD_RES sequence R description Citrulline; alternate => ECO:0000269|PubMed:16567635 source Swiss-Prot : SWS_FT_FI1 36) chain A residue 308 type MOD_RES sequence E description Citrulline; alternate => ECO:0000269|PubMed:16567635 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 310 type MOD_RES sequence R description Citrulline; alternate => ECO:0000269|PubMed:16567635 source Swiss-Prot : SWS_FT_FI1 38) chain A residue 316 type MOD_RES sequence R description Citrulline; alternate => ECO:0000269|PubMed:16567635 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 332 type MOD_RES sequence M description Citrulline; alternate => ECO:0000269|PubMed:16567635 source Swiss-Prot : SWS_FT_FI1 40) chain A residue 801 type MOD_RES sequence E description Citrulline; alternate => ECO:0000269|PubMed:16567635 source Swiss-Prot : SWS_FT_FI1 41) chain A residue 810 type MOD_RES sequence T description Citrulline; alternate => ECO:0000269|PubMed:16567635 source Swiss-Prot : SWS_FT_FI1 42) chain C residue 3 type MOD_RES sequence T description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088 source Swiss-Prot : SWS_FT_FI2 43) chain C residue 4 type MOD_RES sequence M description N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI3 44) chain C residue 5 type MOD_RES sequence Q description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594 source Swiss-Prot : SWS_FT_FI4 45) chain C residue 6 type MOD_RES sequence T description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790 source Swiss-Prot : SWS_FT_FI5 46) chain C residue 8 type MOD_RES sequence R description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433 source Swiss-Prot : SWS_FT_FI6 47) chain C residue 11 type MOD_RES sequence T description Phosphothreonine; by PKC and CHEK1 => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:22901803 source Swiss-Prot : SWS_FT_FI9 48) chain A residue 469 type MOD_RES sequence K description Phosphothreonine; by PKC and CHEK1 => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:22901803 source Swiss-Prot : SWS_FT_FI9

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