eF-site ID 1osv-ABCDE PDB Code 1osv Chain A, B, C, D, E click to enlarge Title STRUCTURAL BASIS FOR BILE ACID BINDING AND ACTIVATION OF THE NUCLEAR RECEPTOR FXR Classification DNA BINDING PROTEIN Compound Bile acid receptor Source Rattus norvegicus (Rat) (NCOA2_MOUSE) Sequence A:  AELTVDQQTLLDYIMDSYSKQRMPQEITNKILKEEFSAEE NFLILTEMATSHVQILVEFTKRLPGFQTLDHEDQIALLKG SAVEAMFLRSAEIFNKKLPAGHADLLEERIRKSGISDEYI TPMFSFYKSVGELKMTQEEYALLTAIVILSPDRQYIKDRE AVEKLQEPLLDVLQKLCKIYQPENPQHFACLLGRLTELRT FNHHHAEMLMSWRVNDHKFTPLLCEIWDV B:  AELTVDQQTLLDYIMDSYSKQRMPQEITNKILKEEFSAEE NFLILTEMATSHVQILVEFTKRLPGFQTLDHEDQIALLKG SAVEAMFLRSAEIFNKKLPAGHADLLEERIRKSGISDEYI TPMFSFYKSVGELKMTQEEYALLTAIVILSPDRQYIKDRE AVEKLQEPLLDVLQKLCKIYQPENPQHFACLLGRLTELRT FNHHHAEMLMSWRVNDHKFTPLLCEIWDV C:  ENALLRYLLDKD D:  ENALLRYLLDKD E:  ENALLRYLLDKD Description Functional site 1) chain B residue 262 type sequence M description BINDING SITE FOR RESIDUE CHC B 201 source : AC1 2) chain B residue 284 type sequence L description BINDING SITE FOR RESIDUE CHC B 201 source : AC1 3) chain B residue 287 type sequence M description BINDING SITE FOR RESIDUE CHC B 201 source : AC1 4) chain B residue 288 type sequence A description BINDING SITE FOR RESIDUE CHC B 201 source : AC1 5) chain B residue 291 type sequence H description BINDING SITE FOR RESIDUE CHC B 201 source : AC1 6) chain B residue 325 type sequence M description BINDING SITE FOR RESIDUE CHC B 201 source : AC1 7) chain B residue 326 type sequence F description BINDING SITE FOR RESIDUE CHC B 201 source : AC1 8) chain B residue 328 type sequence R description BINDING SITE FOR RESIDUE CHC B 201 source : AC1 9) chain B residue 329 type sequence S description BINDING SITE FOR RESIDUE CHC B 201 source : AC1 10) chain B residue 333 type sequence F description BINDING SITE FOR RESIDUE CHC B 201 source : AC1 11) chain B residue 349 type sequence I description BINDING SITE FOR RESIDUE CHC B 201 source : AC1 12) chain B residue 358 type sequence Y description BINDING SITE FOR RESIDUE CHC B 201 source : AC1 13) chain B residue 363 type sequence F description BINDING SITE FOR RESIDUE CHC B 201 source : AC1 14) chain B residue 366 type sequence Y description BINDING SITE FOR RESIDUE CHC B 201 source : AC1 15) chain B residue 444 type sequence H description BINDING SITE FOR RESIDUE CHC B 201 source : AC1 16) chain A residue 262 type sequence M description BINDING SITE FOR RESIDUE CHC A 202 source : AC2 17) chain A residue 325 type sequence M description BINDING SITE FOR RESIDUE CHC A 202 source : AC2 18) chain A residue 326 type sequence F description BINDING SITE FOR RESIDUE CHC A 202 source : AC2 19) chain A residue 328 type sequence R description BINDING SITE FOR RESIDUE CHC A 202 source : AC2 20) chain A residue 329 type sequence S description BINDING SITE FOR RESIDUE CHC A 202 source : AC2 21) chain A residue 349 type sequence I description BINDING SITE FOR RESIDUE CHC A 202 source : AC2 22) chain A residue 358 type sequence Y description BINDING SITE FOR RESIDUE CHC A 202 source : AC2 23) chain A residue 362 type sequence M description BINDING SITE FOR RESIDUE CHC A 202 source : AC2 24) chain A residue 366 type sequence Y description BINDING SITE FOR RESIDUE CHC A 202 source : AC2 25) chain A residue 444 type sequence H description BINDING SITE FOR RESIDUE CHC A 202 source : AC2 26) chain A residue 466 type sequence W description BINDING SITE FOR RESIDUE CHC A 202 source : AC2 27) chain A residue 328 type BINDING sequence R description BINDING => ECO:0000305|PubMed:12718893, ECO:0007744|PDB:1OSV, ECO:0007744|PDB:1OT7 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 358 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:12718893, ECO:0007744|PDB:1OSV, ECO:0007744|PDB:1OT7 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 366 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:12718893, ECO:0007744|PDB:1OSV, ECO:0007744|PDB:1OT7 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 328 type BINDING sequence R description BINDING => ECO:0000305|PubMed:12718893, ECO:0007744|PDB:1OSV, ECO:0007744|PDB:1OT7 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 358 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:12718893, ECO:0007744|PDB:1OSV, ECO:0007744|PDB:1OT7 source Swiss-Prot : SWS_FT_FI1 32) chain B residue 366 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:12718893, ECO:0007744|PDB:1OSV, ECO:0007744|PDB:1OT7 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 444 type BINDING sequence H description BINDING => ECO:0000305|PubMed:12718893, ECO:0007744|PDB:1OSV source Swiss-Prot : SWS_FT_FI2 34) chain B residue 444 type BINDING sequence H description BINDING => ECO:0000305|PubMed:12718893, ECO:0007744|PDB:1OSV source Swiss-Prot : SWS_FT_FI2 35) chain A residue 439 type MOD_RES sequence T description Phosphothreonine; by PKC/PRKCZ => ECO:0000250|UniProtKB:Q96RI1 source Swiss-Prot : SWS_FT_FI3 36) chain B residue 439 type MOD_RES sequence T description Phosphothreonine; by PKC/PRKCZ => ECO:0000250|UniProtKB:Q96RI1 source Swiss-Prot : SWS_FT_FI3 37) chain A residue 272 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0000250|UniProtKB:Q96RI1 source Swiss-Prot : SWS_FT_FI4 38) chain B residue 272 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0000250|UniProtKB:Q96RI1 source Swiss-Prot : SWS_FT_FI4

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