eF-site ID 1kkq-ABCDEFGH PDB Code 1kkq Chain A, B, C, D, E, F, G, H click to enlarge Title Crystal structure of the human PPAR-alpha ligand-binding domain in complex with an antagonist GW6471 and a SMRT corepressor motif Classification TRANSCRIPTION Compound PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR Source Homo sapiens (Human) (NCOR2_HUMAN) Sequence A:  TADLKSLAKRIYEAYLKNFNMNKVKARVILSGKASNNPPF VIHDMETLCMAEKTLVAKLVANGIQNKEAEVRIFHCCQCT SVETVTELTEFAKAIPGFANLDLNDQVTLLKYGVYEAIFA MLSSVMNKDGMLVAYGNGFITREFLKSLRKPFCDIMEPKF DFAMKFNALELDDSDISLFVAAIICCGDRPGLLNVGHIEK MQEGIVHVLRLHLQSNHPDDIFLFPKLLQKMADLRQLVTE HAQLVQIIKKTESDAALHPLLQEIYRDMY B:  TADLKSLAKRIYEAYLKNFNMNKVKARVILSGKASNNPPF VIHDMETLCMAEKTLVAKLVANGIQNKEAEVRIFHCCQCT SVETVTELTEFAKAIPGFANLDLNDQVTLLKYGVYEAIFA MLSSVMNKDGMLVAYGNGFITREFLKSLRKPFCDIMEPKF DFAMKFNALELDDSDISLFVAAIICCGDRPGLLNVGHIEK MQEGIVHVLRLHLQSNHPDDIFLFPKLLQKMADLRQLVTE HAQLVQIIKKTESDAALHPLLQEIYRDMY C:  TADLKSLAKRIYEAYLKNFNMNKVKARVILSGKASNNPPF VIHDMETLCMAEKTLVAKLVANGIQNKEAEVRIFHCCQCT SVETVTELTEFAKAIPGFANLDLNDQVTLLKYGVYEAIFA MLSSVMNKDGMLVAYGNGFITREFLKSLRKPFCDIMEPKF DFAMKFNALELDDSDISLFVAAIICCGDRPGLLNVGHIEK MQEGIVHVLRLHLQSNHPDDIFLFPKLLQKMADLRQLVTE HAQLVQIIKKTESDAALHPLLQEIYRDMY D:  TADLKSLAKRIYEAYLKNFNMNKVKARVILSGKASNNPPF VIHDMETLCMAEKTLVAKLVANGIQNKEAEVRIFHCCQCT SVETVTELTEFAKAIPGFANLDLNDQVTLLKYGVYEAIFA MLSSVMNKDGMLVAYGNGFITREFLKSLRKPFCDIMEPKF DFAMKFNALELDDSDISLFVAAIICCGDRPGLLNVGHIEK MQEGIVHVLRLHLQSNHPDDIFLFPKLLQKMADLRQLVTE HAQLVQIIKKTESDAALHPLLQEIYRDMY E:  NMGLEAIIRKALMGKYDQW F:  NMGLEAIIRKALMGKYDQW G:  NMGLEAIIRKALMGKYDQW H:  NMGLEAIIRKALMGKYDQW Description Functional site 1) chain A residue 254 type sequence L description BINDING SITE FOR RESIDUE 471 A 775 source : AC1 2) chain A residue 269 type sequence E description BINDING SITE FOR RESIDUE 471 A 775 source : AC1 3) chain A residue 272 type sequence I description BINDING SITE FOR RESIDUE 471 A 775 source : AC1 4) chain A residue 273 type sequence F description BINDING SITE FOR RESIDUE 471 A 775 source : AC1 5) chain A residue 275 type sequence C description BINDING SITE FOR RESIDUE 471 A 775 source : AC1 6) chain A residue 276 type sequence C description BINDING SITE FOR RESIDUE 471 A 775 source : AC1 7) chain A residue 280 type sequence S description BINDING SITE FOR RESIDUE 471 A 775 source : AC1 8) chain A residue 314 type sequence Y description BINDING SITE FOR RESIDUE 471 A 775 source : AC1 9) chain A residue 332 type sequence V description BINDING SITE FOR RESIDUE 471 A 775 source : AC1 10) chain A residue 351 type sequence F description BINDING SITE FOR RESIDUE 471 A 775 source : AC1 11) chain A residue 354 type sequence I description BINDING SITE FOR RESIDUE 471 A 775 source : AC1 12) chain A residue 440 type sequence H description BINDING SITE FOR RESIDUE 471 A 775 source : AC1 13) chain A residue 444 type sequence V description BINDING SITE FOR RESIDUE 471 A 775 source : AC1 14) chain A residue 456 type sequence L description BINDING SITE FOR RESIDUE 471 A 775 source : AC1 15) chain B residue 254 type sequence L description BINDING SITE FOR RESIDUE 471 B 776 source : AC2 16) chain B residue 272 type sequence I description BINDING SITE FOR RESIDUE 471 B 776 source : AC2 17) chain B residue 276 type sequence C description BINDING SITE FOR RESIDUE 471 B 776 source : AC2 18) chain B residue 279 type sequence T description BINDING SITE FOR RESIDUE 471 B 776 source : AC2 19) chain B residue 280 type sequence S description BINDING SITE FOR RESIDUE 471 B 776 source : AC2 20) chain B residue 314 type sequence Y description BINDING SITE FOR RESIDUE 471 B 776 source : AC2 21) chain B residue 330 type sequence M description BINDING SITE FOR RESIDUE 471 B 776 source : AC2 22) chain B residue 332 type sequence V description BINDING SITE FOR RESIDUE 471 B 776 source : AC2 23) chain B residue 344 type sequence L description BINDING SITE FOR RESIDUE 471 B 776 source : AC2 24) chain B residue 351 type sequence F description BINDING SITE FOR RESIDUE 471 B 776 source : AC2 25) chain B residue 354 type sequence I description BINDING SITE FOR RESIDUE 471 B 776 source : AC2 26) chain B residue 355 type sequence M description BINDING SITE FOR RESIDUE 471 B 776 source : AC2 27) chain B residue 440 type sequence H description BINDING SITE FOR RESIDUE 471 B 776 source : AC2 28) chain C residue 241 type sequence I description BINDING SITE FOR RESIDUE 471 C 777 source : AC3 29) chain C residue 272 type sequence I description BINDING SITE FOR RESIDUE 471 C 777 source : AC3 30) chain C residue 273 type sequence F description BINDING SITE FOR RESIDUE 471 C 777 source : AC3 31) chain C residue 275 type sequence C description BINDING SITE FOR RESIDUE 471 C 777 source : AC3 32) chain C residue 276 type sequence C description BINDING SITE FOR RESIDUE 471 C 777 source : AC3 33) chain C residue 277 type sequence Q description BINDING SITE FOR RESIDUE 471 C 777 source : AC3 34) chain C residue 279 type sequence T description BINDING SITE FOR RESIDUE 471 C 777 source : AC3 35) chain C residue 280 type sequence S description BINDING SITE FOR RESIDUE 471 C 777 source : AC3 36) chain C residue 314 type sequence Y description BINDING SITE FOR RESIDUE 471 C 777 source : AC3 37) chain C residue 330 type sequence M description BINDING SITE FOR RESIDUE 471 C 777 source : AC3 38) chain C residue 332 type sequence V description BINDING SITE FOR RESIDUE 471 C 777 source : AC3 39) chain C residue 351 type sequence F description BINDING SITE FOR RESIDUE 471 C 777 source : AC3 40) chain C residue 354 type sequence I description BINDING SITE FOR RESIDUE 471 C 777 source : AC3 41) chain C residue 440 type sequence H description BINDING SITE FOR RESIDUE 471 C 777 source : AC3 42) chain D residue 254 type sequence L description BINDING SITE FOR RESIDUE 471 D 778 source : AC4 43) chain D residue 269 type sequence E description BINDING SITE FOR RESIDUE 471 D 778 source : AC4 44) chain D residue 272 type sequence I description BINDING SITE FOR RESIDUE 471 D 778 source : AC4 45) chain D residue 273 type sequence F description BINDING SITE FOR RESIDUE 471 D 778 source : AC4 46) chain D residue 276 type sequence C description BINDING SITE FOR RESIDUE 471 D 778 source : AC4 47) chain D residue 277 type sequence Q description BINDING SITE FOR RESIDUE 471 D 778 source : AC4 48) chain D residue 280 type sequence S description BINDING SITE FOR RESIDUE 471 D 778 source : AC4 49) chain D residue 314 type sequence Y description BINDING SITE FOR RESIDUE 471 D 778 source : AC4 50) chain D residue 330 type sequence M description BINDING SITE FOR RESIDUE 471 D 778 source : AC4 51) chain D residue 332 type sequence V description BINDING SITE FOR RESIDUE 471 D 778 source : AC4 52) chain D residue 344 type sequence L description BINDING SITE FOR RESIDUE 471 D 778 source : AC4 53) chain D residue 351 type sequence F description BINDING SITE FOR RESIDUE 471 D 778 source : AC4 54) chain A residue 433 type SITE sequence L description Essential for heterodimerization with RXRA source Swiss-Prot : SWS_FT_FI2 55) chain B residue 433 type SITE sequence L description Essential for heterodimerization with RXRA source Swiss-Prot : SWS_FT_FI2 56) chain C residue 433 type SITE sequence L description Essential for heterodimerization with RXRA source Swiss-Prot : SWS_FT_FI2 57) chain D residue 433 type SITE sequence L description Essential for heterodimerization with RXRA source Swiss-Prot : SWS_FT_FI2 58) chain A residue 280 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19116277, ECO:0007744|PDB:3ET1 source Swiss-Prot : SWS_FT_FI1 59) chain D residue 280 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19116277, ECO:0007744|PDB:3ET1 source Swiss-Prot : SWS_FT_FI1 60) chain D residue 314 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:19116277, ECO:0007744|PDB:3ET1 source Swiss-Prot : SWS_FT_FI1 61) chain D residue 464 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:19116277, ECO:0007744|PDB:3ET1 source Swiss-Prot : SWS_FT_FI1 62) chain A residue 314 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:19116277, ECO:0007744|PDB:3ET1 source Swiss-Prot : SWS_FT_FI1 63) chain A residue 464 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:19116277, ECO:0007744|PDB:3ET1 source Swiss-Prot : SWS_FT_FI1 64) chain B residue 280 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19116277, ECO:0007744|PDB:3ET1 source Swiss-Prot : SWS_FT_FI1 65) chain B residue 314 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:19116277, ECO:0007744|PDB:3ET1 source Swiss-Prot : SWS_FT_FI1 66) chain B residue 464 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:19116277, ECO:0007744|PDB:3ET1 source Swiss-Prot : SWS_FT_FI1 67) chain C residue 280 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19116277, ECO:0007744|PDB:3ET1 source Swiss-Prot : SWS_FT_FI1 68) chain C residue 314 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:19116277, ECO:0007744|PDB:3ET1 source Swiss-Prot : SWS_FT_FI1 69) chain C residue 464 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:19116277, ECO:0007744|PDB:3ET1 source Swiss-Prot : SWS_FT_FI1

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