eF-site ID 6dha-AB PDB Code 6dha Chain A, B click to enlarge Title Crystal Structure of Human PPARgamma Ligand Binding Domain in Complex with Hydroxy Pioglitazone (M-IV) Classification transcription/transcription inhibitor Compound Peroxisome proliferator-activated receptor gamma Source (PPARG_HUMAN) Sequence A:  ESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSP FVIYDMNSLMMGEDEVAIRIFQGCQFRSVEAVQEITEYAK SIPGFVNLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLI SEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDD SDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQL KLNHPESSQLFAKLLQKMTDLRQIVTEHVQLLQVIKKTET DMSLHPLLQEIYKDL B:  ESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSP FVIYDMNSLMMGEDKIKFKHITEVAIRIFQGCQFRSVEAV QEITEYAKSIPGFVNLDLNDQVTLLKYGVHEIIYTMLASL MNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVK FNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNL LQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQLL QVIKKTETDMSLHPLLQEIYKDL Description Functional site 1) chain A residue 281 type sequence I description binding site for residue GFV A 501 source : AC1 2) chain A residue 282 type sequence F description binding site for residue GFV A 501 source : AC1 3) chain A residue 284 type sequence G description binding site for residue GFV A 501 source : AC1 4) chain A residue 285 type sequence C description binding site for residue GFV A 501 source : AC1 5) chain A residue 286 type sequence Q description binding site for residue GFV A 501 source : AC1 6) chain A residue 289 type sequence S description binding site for residue GFV A 501 source : AC1 7) chain A residue 323 type sequence H description binding site for residue GFV A 501 source : AC1 8) chain A residue 327 type sequence Y description binding site for residue GFV A 501 source : AC1 9) chain A residue 330 type sequence L description binding site for residue GFV A 501 source : AC1 10) chain A residue 341 type sequence I description binding site for residue GFV A 501 source : AC1 11) chain A residue 364 type sequence M description binding site for residue GFV A 501 source : AC1 12) chain A residue 449 type sequence H description binding site for residue GFV A 501 source : AC1 13) chain A residue 473 type sequence Y description binding site for residue GFV A 501 source : AC1 14) chain A residue 228 type sequence L description binding site for residue KNA A 502 source : AC2 15) chain A residue 288 type sequence R description binding site for residue KNA A 502 source : AC2 16) chain A residue 329 type sequence M description binding site for residue KNA A 502 source : AC2 17) chain A residue 330 type sequence L description binding site for residue KNA A 502 source : AC2 18) chain A residue 333 type sequence L description binding site for residue KNA A 502 source : AC2 19) chain A residue 342 type sequence S description binding site for residue KNA A 502 source : AC2 20) chain A residue 343 type sequence E description binding site for residue KNA A 502 source : AC2 21) chain A residue 258 type sequence G description binding site for residue KNA A 503 source : AC3 22) chain B residue 249 type sequence I description binding site for residue GFV B 501 source : AC4 23) chain B residue 255 type sequence L description binding site for residue GFV B 501 source : AC4 24) chain B residue 259 type sequence E description binding site for residue GFV B 501 source : AC4 25) chain B residue 264 type sequence F description binding site for residue GFV B 501 source : AC4 26) chain B residue 266 type sequence H description binding site for residue GFV B 501 source : AC4 27) chain B residue 267 type sequence I description binding site for residue GFV B 501 source : AC4 28) chain B residue 280 type sequence R description binding site for residue GFV B 501 source : AC4 29) chain B residue 281 type sequence I description binding site for residue GFV B 501 source : AC4 30) chain B residue 285 type sequence C description binding site for residue GFV B 501 source : AC4 31) chain B residue 288 type sequence R description binding site for residue GFV B 501 source : AC4 32) chain B residue 292 type sequence A description binding site for residue GFV B 501 source : AC4 33) chain B residue 326 type sequence I description binding site for residue GFV B 501 source : AC4 34) chain B residue 330 type sequence L description binding site for residue GFV B 501 source : AC4 35) chain B residue 341 type sequence I description binding site for residue GFV B 501 source : AC4 36) chain B residue 348 type sequence M description binding site for residue GFV B 501 source : AC4 37) chain A residue 286 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:9744270, ECO:0007744|PDB:2PRG source Swiss-Prot : SWS_FT_FI1 38) chain A residue 323 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9744270, ECO:0007744|PDB:2PRG source Swiss-Prot : SWS_FT_FI1 39) chain A residue 449 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9744270, ECO:0007744|PDB:2PRG source Swiss-Prot : SWS_FT_FI1 40) chain A residue 473 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:9744270, ECO:0007744|PDB:2PRG source Swiss-Prot : SWS_FT_FI1 41) chain B residue 286 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:9744270, ECO:0007744|PDB:2PRG source Swiss-Prot : SWS_FT_FI1 42) chain B residue 323 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9744270, ECO:0007744|PDB:2PRG source Swiss-Prot : SWS_FT_FI1 43) chain B residue 449 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9744270, ECO:0007744|PDB:2PRG source Swiss-Prot : SWS_FT_FI1 44) chain B residue 473 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:9744270, ECO:0007744|PDB:2PRG source Swiss-Prot : SWS_FT_FI1 45) chain A residue 224 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:36737649 source Swiss-Prot : SWS_FT_FI2 46) chain B residue 224 type CROSSLNK sequence K 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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