eF-site ID 1prg-A PDB Code 1prg Chain A click to enlarge Title LIGAND BINDING DOMAIN OF THE HUMAN PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA Classification GENE REGULATION Compound PROTEIN (PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA) Source Homo sapiens (Human) (PPAT_HUMAN) Sequence A:  ESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSP FVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQ FRSVEAVQEITEYAKSIPGFVNLDLNDQVTLLKYGVHEII YTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEP KFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPI EDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIV TEHVQLLQVIKKTETDMSLHPLLQEIYKDL Description Functional site 1) chain A residue 323 type sequence H description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LND 2) chain A residue 469 type sequence L description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LND 3) chain A residue 449 type sequence H description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LND 4) chain A residue 286 type sequence Q description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LND 5) chain A residue 327 type sequence Y description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LND 6) chain A residue 330 type sequence L description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LND 7) chain A residue 282 type sequence F description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LND 8) chain A residue 285 type sequence C description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LND 9) chain A residue 288 type sequence R description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LND 10) chain A residue 339 type sequence V description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LND 11) chain A residue 341 type sequence I description THESE RESIDUES ARE INVOLVED IN LIGAND BINDING. source : LND 12) chain A residue 471 type sequence E description THESE RESIDUES ARE INVOLVED IN BINDING THE LXXLL HELIX OF COACTIVATORS. source : LLL 13) chain A residue 301 type sequence K description THESE RESIDUES ARE INVOLVED IN BINDING THE LXXLL HELIX OF COACTIVATORS. source : LLL 14) chain A residue 297 type sequence T description THESE RESIDUES ARE INVOLVED IN BINDING THE LXXLL HELIX OF COACTIVATORS. source : LLL 15) chain A residue 314 type sequence Q description THESE RESIDUES ARE INVOLVED IN BINDING THE LXXLL HELIX OF COACTIVATORS. source : LLL 16) chain A residue 315 type sequence V description THESE RESIDUES ARE INVOLVED IN BINDING THE LXXLL HELIX OF COACTIVATORS. source : LLL 17) chain A residue 468 type sequence L description THESE RESIDUES ARE INVOLVED IN BINDING THE LXXLL HELIX OF COACTIVATORS. source : LLL 18) chain A residue 318 type sequence L description THESE RESIDUES ARE INVOLVED IN BINDING THE LXXLL HELIX OF COACTIVATORS. source : LLL 19) chain A residue 311 type sequence L description THESE RESIDUES ARE INVOLVED IN BINDING THE LXXLL HELIX OF COACTIVATORS. source : LLL 20) chain A residue 316 type BINDING sequence T description BINDING => ECO:0000269|PubMed:9744270, ECO:0007744|PDB:2PRG source Swiss-Prot : SWS_FT_FI1 21) chain A residue 353 type BINDING sequence L description BINDING => ECO:0000269|PubMed:9744270, ECO:0007744|PDB:2PRG source Swiss-Prot : SWS_FT_FI1 22) 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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