eF-site ID 2prg-B PDB Code 2prg Chain B 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 B:  ESADLRALAKHLYDSYIKSFPLTKAKARAILTVIYDMNSL MQSKEVAIRIFQGCQFRSVEAVQEITEYAKSIPGFVNLDL NDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTRE FLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVI ILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQL FAKLLQKMTDLRQIVTEHVQLLQVIKKTETDMSLHPLLQE IYKDLY Description Functional site 1) chain B residue 323 type sequence H description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB2 2) chain B residue 469 type sequence L description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB2 3) chain B residue 449 type sequence H description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB2 4) chain B residue 286 type sequence Q description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB2 5) chain B residue 327 type sequence Y description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB2 6) chain B residue 330 type sequence L description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB2 7) chain B residue 282 type sequence F description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB2 8) chain B residue 285 type sequence C description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB2 9) chain B residue 288 type sequence R description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB2 10) chain B residue 338 type sequence G description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB2 11) chain B residue 341 type sequence I description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LB2 12) chain B residue 471 type sequence E description RESIDUES INVOLVED IN BINDING THE COACTIVATOR LXXLL HELIX. source : CA2 13) chain B residue 301 type sequence K description RESIDUES INVOLVED IN BINDING THE COACTIVATOR LXXLL HELIX. source : CA2 14) chain B residue 297 type sequence T description RESIDUES INVOLVED IN BINDING THE COACTIVATOR LXXLL HELIX. source : CA2 15) chain B residue 314 type sequence Q description RESIDUES INVOLVED IN BINDING THE COACTIVATOR LXXLL HELIX. source : CA2 16) chain B residue 315 type sequence V description RESIDUES INVOLVED IN BINDING THE COACTIVATOR LXXLL HELIX. source : CA2 17) chain B residue 468 type sequence L description RESIDUES INVOLVED IN BINDING THE COACTIVATOR LXXLL HELIX. source : CA2 18) chain B residue 318 type sequence L description RESIDUES INVOLVED IN BINDING THE COACTIVATOR LXXLL HELIX. source : CA2 19) chain B residue 311 type sequence L description RESIDUES INVOLVED IN BINDING THE COACTIVATOR LXXLL HELIX. source : CA2 20) chain B residue 282 type sequence F description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 21) chain B residue 285 type sequence C description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 22) chain B residue 286 type sequence Q description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 23) chain B residue 289 type sequence S description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 24) chain B residue 323 type sequence H description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 25) chain B residue 327 type sequence Y description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 26) chain B residue 330 type sequence L description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 27) chain B residue 340 type sequence L description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 28) chain B residue 341 type sequence I description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 29) chain B residue 364 type sequence M description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 30) chain B residue 449 type sequence H description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 31) chain B residue 453 type sequence L description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 32) chain B residue 473 type sequence Y description BINDING SITE FOR RESIDUE BRL B 2 source : AC2 33) chain B residue 316 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 34) chain B residue 353 type MOD_RES sequence L description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 35) 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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