eF-site ID 5i6c-AB PDB Code 5i6c Chain A, B click to enlarge Title The structure of the eukaryotic purine/H+ symporter, UapA, in complex with Xanthine Classification TRANSPORT PROTEIN Compound Uric acid-xanthine permease Source Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) (UAPA_EMENI) Sequence A:  PFFGLNEKIPVLLAFILGLQHALAMLAGVVTPPLIISSSL SLPSDLQQYLVSTSLIVCGLLSMVQITRFHIYKTPYYIGS GVLSVMGVSFSIISVASGAFNQMYSNGFCQLDEAGNRLPC PEAYGALIGTSACCALVEILLAFVPPKVIQKIFPPIVTGP TVMLIGISLIGTGFKDWAGGSACMDDGMLCPSATAPRPLP WGSPEFIGLGFLVFVSIILCERFGAPIMKSCSVVIGLLVG CIVAAACGYFSHADIDAAPAASFIWVKTFPLSVYGPMVLP IIAVFIICACECIGDVTATCDVSRLEVRGGTFESRIQGAV LADGINSVVAALATMTPMTTFAQNNVVIALTRCANRWAGY CCCLILIVAGIFAKFAAAIVAIPNSVMGGMKTFLFASVVI SGQAIVAKAPFTRRNRFILTASMALGYGATLVPTWFGNVF PQTENRDLEGFENAIELVLETGFAVTAFVAMLLNAIMPAE B:  PFFGLNEKIPVLLAFILGLQHALAMLAGVVTPPLIISSSL SLPSDLQQYLVSTSLIVCGLLSMVQITSGVLSVMGVSFSI ISVASGAFNQMYSNGFCQLDEAGNRLPCPEAYGALIGTSA CCALVEILLAFVPPKVIQKIFPPIVTGPTVMLIGISLIGT GFKDWAGGSACMDDGMLCPSATAPRPLPWGSPEFIGLGFL VFVSIILCERFGAPIMKSCSVVIGLLVGCIVAAACGYFSH ADIDAAPAASFIWVKTFPLSVYGPMVLPIIAVFIICACEC IGDVTATCDVSRLEVRGGTFESRIQGAVLADGINSVVAAL ATMTPMTTFAQNNVVIALTRCANRWAGYCCCLILIVAGIF AKFAAAIVAIPNSVMGGMKTFLFASVVISGQAIVAKAPFT RRNRFILTASMALGYGATLVPTWFGNVFPQTENRDLEGFE NAIELVLETGFAVTAFVAMLLNAIMPAE Description (1)  Uric acid-xanthine permease Functional site 1) chain A residue 93 type sequence G description binding site for residue XAN A 1001 source : AC1 2) chain A residue 153 type sequence V description binding site for residue XAN A 1001 source : AC1 3) chain A residue 154 type sequence S description binding site for residue XAN A 1001 source : AC1 4) chain A residue 155 type sequence F description binding site for residue XAN A 1001 source : AC1 5) chain A residue 356 type sequence E description binding site for residue XAN A 1001 source : AC1 6) chain A residue 404 type sequence T description binding site for residue XAN A 1001 source : AC1 7) chain A residue 406 type sequence F description binding site for residue XAN A 1001 source : AC1 8) chain A residue 407 type sequence A description binding site for residue XAN A 1001 source : AC1 9) chain A residue 408 type sequence Q description binding site for residue XAN A 1001 source : AC1 10) chain A residue 223 type sequence T description binding site for residue LMT A 1002 source : AC2 11) chain A residue 227 type sequence V description binding site for residue LMT A 1002 source : AC2 12) chain A residue 348 type sequence A description binding site for residue LMT A 1002 source : AC2 13) chain A residue 352 type sequence I description binding site for residue LMT A 1002 source : AC2 14) chain A residue 355 type sequence C description binding site for residue LMT A 1002 source : AC2 15) chain A residue 360 type sequence D description binding site for residue LMT A 1002 source : AC2 16) chain A residue 363 type sequence A description binding site for residue LMT A 1002 source : AC2 17) chain A residue 407 type sequence A description binding site for residue LMT A 1002 source : AC2 18) chain A residue 473 type sequence K description binding site for residue LMT A 1002 source : AC2 19) chain A residue 529 type sequence A description binding site for residue LMT A 1002 source : AC2 20) chain A residue 89 type sequence A description binding site for residue LMT A 1003 source : AC3 21) chain A residue 295 type sequence S description binding site for residue LMT A 1003 source : AC3 22) chain A residue 298 type sequence V description binding site for residue LMT A 1003 source : AC3 23) chain A residue 356 type sequence E description binding site for residue LMT A 1003 source : AC3 24) chain A residue 408 type sequence Q description binding site for residue LMT A 1003 source : AC3 25) chain A residue 459 type sequence L description binding site for residue LMT A 1003 source : AC3 26) chain A residue 462 type sequence S description binding site for residue LMT A 1003 source : AC3 27) chain A residue 466 type sequence S description binding site for residue LMT A 1003 source : AC3 28) chain B residue 478 type sequence R description binding site for residue LMT A 1003 source : AC3 29) chain B residue 153 type sequence V description binding site for residue XAN B 1001 source : AC4 30) chain B residue 154 type sequence S description binding site for residue XAN B 1001 source : AC4 31) chain B residue 155 type sequence F description binding site for residue XAN B 1001 source : AC4 32) chain B residue 356 type sequence E description binding site for residue XAN B 1001 source : AC4 33) chain B residue 405 type sequence T description binding site for residue XAN B 1001 source : AC4 34) chain B residue 406 type sequence F description binding site for residue XAN B 1001 source : AC4 35) chain B residue 407 type sequence A description binding site for residue XAN B 1001 source : AC4 36) chain B residue 408 type sequence Q description binding site for residue XAN B 1001 source : AC4 37) chain B residue 223 type sequence T description binding site for residue LMT B 1002 source : AC5 38) chain B residue 227 type sequence V description binding site for residue LMT B 1002 source : AC5 39) chain B residue 348 type sequence A description binding site for residue LMT B 1002 source : AC5 40) chain B residue 352 type sequence I description binding site for residue LMT B 1002 source : AC5 41) chain B residue 355 type sequence C description binding site for residue LMT B 1002 source : AC5 42) chain B residue 407 type sequence A description binding site for residue LMT B 1002 source : AC5 43) chain B residue 466 type sequence S description binding site for residue LMT B 1002 source : AC5 44) chain B residue 470 type sequence I description binding site for residue LMT B 1002 source : AC5 45) chain B residue 473 type sequence K description binding site for residue LMT B 1002 source : AC5 46) chain B residue 529 type sequence A description binding site for residue LMT B 1002 source : AC5 47) chain A residue 478 type sequence R description binding site for residue LMT B 1003 source : AC6 48) chain B residue 89 type sequence A description binding site for residue LMT B 1003 source : AC6 49) chain B residue 295 type sequence S description binding site for residue LMT B 1003 source : AC6 50) chain B residue 298 type sequence V description binding site for residue LMT B 1003 source : AC6 51) chain B residue 356 type sequence E description binding site for residue LMT B 1003 source : AC6 52) chain B residue 408 type sequence Q description binding site for residue LMT B 1003 source : AC6 53) chain B residue 459 type sequence L description binding site for residue LMT B 1003 source : AC6 54) chain B residue 462 type sequence S description binding site for residue LMT B 1003 source : AC6 55) chain B residue 466 type sequence S description binding site for residue LMT B 1003 source : AC6 56) chain A residue 447-467 type prosite sequence IPNSVMGGMKTFLFASVVISG description XANTH_URACIL_PERMASE Xanthine/uracil permeases family signature. IPnSVMGGmktfLFAsVvisG source prosite : PS01116 57) chain A residue 77-97 type TRANSMEM sequence LLAFILGLQHALAMLAGVVTP description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 58) chain A residue 451-471 type TRANSMEM sequence VMGGMKTFLFASVVISGQAIV description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 59) chain A residue 482-502 type TRANSMEM sequence FILTASMALGYGATLVPTWFG description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 60) chain A residue 522-542 type TRANSMEM sequence LVLETGFAVTAFVAMLLNAIM description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 61) chain B residue 77-97 type TRANSMEM sequence LLAFILGLQHALAMLAGVVTP description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 62) chain B residue 111-131 type TRANSMEM sequence LQQYLVSTSLIVCGLLSMVQI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 63) chain B residue 188-209 type TRANSMEM sequence AYGALIGTSACCALVEILLAFV description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 64) chain B residue 217-237 type TRANSMEM sequence IFPPIVTGPTVMLIGISLIGT description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 65) chain B residue 264-284 type TRANSMEM sequence LPWGSPEFIGLGFLVFVSIIL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 66) chain B residue 296-315 type TRANSMEM sequence CSVVIGLLVGCIVAAACGYF description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 67) chain A residue 111-131 type TRANSMEM sequence LQQYLVSTSLIVCGLLSMVQI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 68) chain B residue 338-361 type TRANSMEM sequence VYGPMVLPIIAVFIICACECIGDV description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 69) chain B residue 427-447 type TRANSMEM sequence CCLILIVAGIFAKFAAAIVAI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 70) chain B residue 451-471 type TRANSMEM sequence VMGGMKTFLFASVVISGQAIV description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 71) chain B residue 482-502 type TRANSMEM sequence FILTASMALGYGATLVPTWFG description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 72) chain B residue 522-542 type TRANSMEM sequence LVLETGFAVTAFVAMLLNAIM description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 73) chain A residue 141-161 type TRANSMEM sequence YYIGSGVLSVMGVSFSIISVA description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 74) chain A residue 188-209 type TRANSMEM sequence AYGALIGTSACCALVEILLAFV description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 75) chain A residue 217-237 type TRANSMEM sequence IFPPIVTGPTVMLIGISLIGT description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 76) chain A residue 264-284 type TRANSMEM sequence LPWGSPEFIGLGFLVFVSIIL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 77) chain A residue 296-315 type TRANSMEM sequence CSVVIGLLVGCIVAAACGYF description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 78) chain A residue 338-361 type TRANSMEM sequence VYGPMVLPIIAVFIICACECIGDV description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 79) chain A residue 427-447 type TRANSMEM sequence CCLILIVAGIFAKFAAAIVAI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1

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