eF-site ID 2prg-A PDB Code 2prg Chain A 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 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 A residue 471 type sequence E description RESIDUES INVOLVED IN BINDING THE LXXLL COACTIVATOR HELIX. source : CA1 13) chain A residue 301 type sequence K description RESIDUES INVOLVED IN BINDING THE LXXLL COACTIVATOR HELIX. source : CA1 14) chain A residue 297 type sequence T description RESIDUES INVOLVED IN BINDING THE LXXLL COACTIVATOR HELIX. source : CA1 15) chain A residue 314 type sequence Q description RESIDUES INVOLVED IN BINDING THE LXXLL COACTIVATOR HELIX. source : CA1 16) chain A residue 315 type sequence V description RESIDUES INVOLVED IN BINDING THE LXXLL COACTIVATOR HELIX. source : CA1 17) chain A residue 468 type sequence L description RESIDUES INVOLVED IN BINDING THE LXXLL COACTIVATOR HELIX. source : CA1 18) chain A residue 318 type sequence L description RESIDUES INVOLVED IN BINDING THE LXXLL COACTIVATOR HELIX. source : CA1 19) chain A residue 311 type sequence L description RESIDUES INVOLVED IN BINDING THE LXXLL COACTIVATOR HELIX. source : CA1 20) chain A residue 282 type sequence F description BINDING SITE FOR RESIDUE BRL A 1 source : AC1 21) chain A residue 284 type sequence G description BINDING SITE FOR RESIDUE BRL A 1 source : AC1 22) chain A residue 285 type sequence C description BINDING SITE FOR RESIDUE BRL A 1 source : AC1 23) chain A residue 286 type sequence Q description BINDING SITE FOR RESIDUE BRL A 1 source : AC1 24) chain A residue 289 type sequence S description BINDING SITE FOR RESIDUE BRL A 1 source : AC1 25) chain A residue 323 type sequence H description BINDING SITE FOR RESIDUE BRL A 1 source : AC1 26) chain A residue 327 type sequence Y description BINDING SITE FOR RESIDUE BRL A 1 source : AC1 27) chain A residue 341 type sequence I description BINDING SITE FOR RESIDUE BRL A 1 source : AC1 28) chain A residue 364 type sequence M description BINDING SITE FOR RESIDUE BRL A 1 source : AC1 29) chain A residue 449 type sequence H description BINDING SITE FOR RESIDUE BRL A 1 source : AC1 30) chain A residue 473 type sequence Y description BINDING SITE FOR RESIDUE BRL A 1 source : AC1 31) chain A residue 353 type MOD_RES sequence L description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 32) 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

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