eF-site ID 2prg-ABC PDB Code 2prg Chain A, B, C click to enlarge Title LIGAND-BINDING DOMAIN OF THE HUMAN PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA Classification COMPLEX (THIAZOLIDINEDIONE/RECEPTOR) Compound PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA Source (O43792) Sequence A:  ESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSP FVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQ FRSVEAVQEITEYAKSIPGFVNLDLNDQVTLLKYGVHEII YTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEP KFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPI EDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIV TEHVQLLQVIKKTETDMSLHPLLQEIYKDLY B:  ESADLRALAKHLYDSYIKSFPLTKAKARAILTVIYDMNSL MQSKEVAIRIFQGCQFRSVEAVQEITEYAKSIPGFVNLDL NDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTRE FLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVI ILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQL FAKLLQKMTDLRQIVTEHVQLLQVIKKTETDMSLHPLLQE IYKDLY C:  QTSHKLVQLLTTTERHKILHRLLQEGSPSDIT Description Functional site 1) chain A residue 323 type sequence H description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB1 2) chain A residue 469 type sequence L description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB1 3) chain A residue 449 type sequence H description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB1 4) chain A residue 286 type sequence Q description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB1 5) chain A residue 327 type sequence Y description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB1 6) chain A residue 330 type sequence L description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB1 7) chain A residue 282 type sequence F description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB1 8) chain A residue 285 type sequence C description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB1 9) chain A residue 288 type sequence R description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB1 10) chain A residue 338 type sequence G description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB1 11) chain A residue 341 type sequence I description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB1 12) chain B residue 323 type sequence H description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB2 13) chain B residue 469 type sequence L description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB2 14) chain B residue 449 type sequence H description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB2 15) chain B residue 286 type sequence Q description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB2 16) chain B residue 327 type sequence Y description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB2 17) chain B residue 330 type sequence L description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB2 18) chain B residue 282 type sequence F description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB2 19) chain B residue 285 type sequence C description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB2 20) chain B residue 288 type sequence R description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB2 21) chain B residue 338 type sequence G description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB2 22) chain B residue 341 type sequence I description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB2 23) chain A residue 471 type sequence E description RESIDUES INVOLVED IN BINDING THE LXXLL COACTIVATOR HELIX. source : CA1 24) chain A residue 301 type sequence K description RESIDUES INVOLVED IN BINDING THE LXXLL COACTIVATOR HELIX. source : CA1 25) chain A residue 297 type sequence T description RESIDUES INVOLVED IN BINDING THE LXXLL COACTIVATOR HELIX. source : CA1 26) chain A residue 314 type sequence Q description RESIDUES INVOLVED IN BINDING THE LXXLL COACTIVATOR HELIX. source : CA1 27) chain A residue 315 type sequence V description RESIDUES INVOLVED IN BINDING THE LXXLL COACTIVATOR HELIX. source : CA1 28) chain A residue 468 type sequence L description RESIDUES INVOLVED IN BINDING THE LXXLL COACTIVATOR HELIX. source : CA1 29) chain A residue 318 type sequence L description RESIDUES INVOLVED IN BINDING THE LXXLL COACTIVATOR HELIX. source : CA1 30) chain A residue 311 type sequence L description RESIDUES INVOLVED IN BINDING THE LXXLL COACTIVATOR HELIX. source : CA1 31) chain B residue 471 type sequence E description RESIDUES INVOLVED IN BINDING THE COACTIVATOR LXXLL HELIX. source : CA2 32) chain B residue 301 type sequence K description RESIDUES INVOLVED IN BINDING THE COACTIVATOR LXXLL HELIX. source : CA2 33) chain B residue 297 type sequence T description RESIDUES INVOLVED IN BINDING THE COACTIVATOR LXXLL HELIX. source : CA2 34) chain B residue 314 type sequence Q description RESIDUES INVOLVED IN BINDING THE COACTIVATOR LXXLL HELIX. source : CA2 35) chain B residue 315 type sequence V description RESIDUES INVOLVED IN BINDING THE COACTIVATOR LXXLL HELIX. source : CA2 36) chain B residue 468 type sequence L description RESIDUES INVOLVED IN BINDING THE COACTIVATOR LXXLL HELIX. source : CA2 37) chain B residue 318 type sequence L description RESIDUES INVOLVED IN BINDING THE COACTIVATOR LXXLL HELIX. source : CA2 38) chain B residue 311 type sequence L description RESIDUES INVOLVED IN BINDING THE COACTIVATOR LXXLL HELIX. source : CA2 39) chain A residue 282 type sequence F description BINDING SITE FOR RESIDUE BRL A 1 source : AC1 40) chain A residue 284 type sequence G description BINDING SITE FOR RESIDUE BRL A 1 source : AC1 41) chain A residue 285 type sequence C description BINDING SITE FOR RESIDUE BRL A 1 source : AC1 42) chain A residue 286 type sequence Q description BINDING SITE FOR RESIDUE BRL A 1 source : AC1 43) chain A residue 289 type sequence S description BINDING SITE FOR RESIDUE BRL A 1 source : AC1 44) chain A residue 323 type sequence H description BINDING SITE FOR RESIDUE BRL A 1 source : AC1 45) chain A residue 327 type sequence Y description BINDING SITE FOR RESIDUE BRL A 1 source : AC1 46) chain A residue 341 type sequence I description BINDING SITE FOR RESIDUE BRL A 1 source : AC1 47) chain A residue 364 type sequence M description BINDING SITE FOR RESIDUE BRL A 1 source : AC1 48) chain A residue 449 type sequence H description BINDING SITE FOR RESIDUE BRL A 1 source : AC1 49) chain A residue 473 type sequence Y description BINDING SITE FOR RESIDUE BRL A 1 source : AC1 50) chain B residue 282 type sequence F description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 51) chain B residue 285 type sequence C description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 52) chain B residue 286 type sequence Q description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 53) chain B residue 289 type sequence S description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 54) chain B residue 323 type sequence H description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 55) chain B residue 327 type sequence Y description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 56) chain B residue 330 type sequence L description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 57) chain B residue 340 type sequence L description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 58) chain B residue 341 type sequence I description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 59) chain B residue 364 type sequence M description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 60) chain B residue 449 type sequence H description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 61) chain B residue 453 type sequence L description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 62) chain B residue 473 type sequence Y description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 63) chain C residue 698 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 64) chain A residue 353 type MOD_RES sequence L description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 65) chain B residue 316 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 66) chain B residue 353 type MOD_RES sequence L description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 67) chain A residue 254 type CROSSLNK sequence S description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:36737649 source Swiss-Prot : SWS_FT_FI2 68) chain B residue 254 type CROSSLNK sequence S description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:36737649 source Swiss-Prot : SWS_FT_FI2

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