eF-site ID 4ytz-A PDB Code 4ytz Chain A click to enlarge Title Rat xanthine oxidoreductase, C-terminal deletion protein variant, crystal grown without dithiothreitol Classification OXIDOREDUCTASE Compound Xanthine dehydrogenase/oxidase Source (XDH_RAT) Sequence A:  ADELVFFVNGKKVVEKNADPETTLLVYLRRKLGLCGTKLG CGEGGCGACTVMISKYDRLQNKIVHFSVNACLAPICSLHH VAVTTVEGIGNTQKLHPVQERIARSHGSQCGFCTPGIVMS MYTLLRNQPEPTVEEIENAFQGNLCRCTGYRPILQGFRTF AKDLSPSLFNPEDFKPLDPTQEPIFPPELLRLKDTPQKKL RFEGERVTWIQASTMEELLDLKAQHPDAKLVVGNTEIGIE MKFKNMLFPLIVCPAWIPELNSVVHGPEGISFGASCPLSL VESVLAEEIAKLPEQKTEVFRGVMEQLRWFAGKQVKSVAS IGGNIITASPISDLNPVFMASGAKLTLVSRGTRRTVRMDH TFFPGYRKTLLRPEEILLSIEIPYSKEGEFFSAFKQASRR EDDIAKVTSGMRVLFKPGTIEVQELSLCFGGMADRTISAL KTTPKQLSKSWNEELLQSVCAGLAEELQLAPDAPGGMVEF RRTLTLSFFFKFYLTVLQKLGRADLEDMCGKLDPTFASAT LLFQKDPPANVQLFQEVPKDQSEEDMVGRPLPHLAANMQA SGEAVYCDDIPRYENELSLRLVTSTRAHAKITSIDTSEAK KVPGFVCFLTAEDVPNSNATGLFNDETVFAKDEVTCVGHI IGAVVADTPEHAQRAARGVKITYEDLPAIITIQDAINNNS FYGSEIKIEKGDLKKGFSEADNVVSGELYIGGQEHFYLET NCTIAVPKGEAGEMELFVSTQNTMKTQSFVAKMLGVPDNR IVVRVKRMGGGFGGKETRSTVVSTALALAAHKTGRPVRCM LDRDEDMLITGGRHPFLAKYKVGFMKTGTVVALEVAHFSN GGNTEDLSRSIMERALFHMDNAYKIPNIRGTGRICKTNLP SNTAFRGFGGPQGMLIAEYWMSEVAITCGLPAEEVRRKNM YKEGDLTHFNQKLEGFTLPRCWDECIASSQYLARKREVEK FNRENCWKKRGLCIIPTKFGISFTLPFLNQGGALVHVYTD GSVLLTHGGTEMGQGLHTKMVQVASRALKIPTSKIHISET STNTVPNTSPTAASASADLNGQGVYEACQTILKRLEPFKK KKPTGPWEAWVMDAYTSAVSLSATGFYKTPNLGYSFETNS GNPFHYFSYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSL NPAIDIGQVEGAFVQGLGLFTMEELHYSPEGSLHTRGPST YKIPAFGSIPIEFRVSLLRDCPNKRAIYASKAVGEPPLFL ASSIFFAIKDAIRAARAQHGDNAKQLFQLDSPATPEKIRN ACVDQFTTL Description Functional site 1) chain A residue 111 type sequence Q description binding site for residue FES A 1401 source : AC1 2) chain A residue 112 type sequence C description binding site for residue FES A 1401 source : AC1 3) chain A residue 113 type sequence G description binding site for residue FES A 1401 source : AC1 4) chain A residue 115 type sequence C description binding site for residue FES A 1401 source : AC1 5) chain A residue 147 type sequence C description binding site for residue FES A 1401 source : AC1 6) chain A residue 148 type sequence R description binding site for residue FES A 1401 source : AC1 7) chain A residue 149 type sequence C description binding site for residue FES A 1401 source : AC1 8) chain A residue 42 type sequence G description binding site for residue FES A 1402 source : AC2 9) chain A residue 43 type sequence C description binding site for residue FES A 1402 source : AC2 10) chain A residue 44 type sequence G description binding site for residue FES A 1402 source : AC2 11) chain A residue 46 type sequence G description binding site for residue FES A 1402 source : AC2 12) chain A residue 47 type sequence G description binding site for residue FES A 1402 source : AC2 13) chain A residue 48 type sequence C description binding site for residue FES A 1402 source : AC2 14) chain A residue 49 type sequence G description binding site for residue FES A 1402 source : AC2 15) chain A residue 51 type sequence C description binding site for residue FES A 1402 source : AC2 16) chain A residue 71 type sequence N description binding site for residue FES A 1402 source : AC2 17) chain A residue 73 type sequence C description binding site for residue FES A 1402 source : AC2 18) chain A residue 46 type sequence G description binding site for residue FAD A 1403 source : AC3 19) chain A residue 256 type sequence L description binding site for residue FAD A 1403 source : AC3 20) chain A residue 257 type sequence V description binding site for residue FAD A 1403 source : AC3 21) chain A residue 258 type sequence V description binding site for residue FAD A 1403 source : AC3 22) chain A residue 259 type sequence G description binding site for residue FAD A 1403 source : AC3 23) chain A residue 260 type sequence N description binding site for residue FAD A 1403 source : AC3 24) chain A residue 261 type sequence T description binding site for residue FAD A 1403 source : AC3 25) chain A residue 262 type sequence E description binding site for residue FAD A 1403 source : AC3 26) chain A residue 263 type sequence I description binding site for residue FAD A 1403 source : AC3 27) chain A residue 300 type sequence A description binding site for residue FAD A 1403 source : AC3 28) chain A residue 336 type sequence F description binding site for residue FAD A 1403 source : AC3 29) chain A residue 337 type sequence A description binding site for residue FAD A 1403 source : AC3 30) chain A residue 345 type sequence A description binding site for residue FAD A 1403 source : AC3 31) chain A residue 346 type sequence S description binding site for residue FAD A 1403 source : AC3 32) chain A residue 349 type sequence G description binding site for residue FAD A 1403 source : AC3 33) chain A residue 350 type sequence N description binding site for residue FAD A 1403 source : AC3 34) chain A residue 352 type sequence I description binding site for residue FAD A 1403 source : AC3 35) chain A residue 353 type sequence T description binding site for residue FAD A 1403 source : AC3 36) chain A residue 358 type sequence S description binding site for residue FAD A 1403 source : AC3 37) chain A residue 359 type sequence D description binding site for residue FAD A 1403 source : AC3 38) chain A residue 402 type sequence I description binding site for residue FAD A 1403 source : AC3 39) chain A residue 403 type sequence L description binding site for residue FAD A 1403 source : AC3 40) chain A residue 802 type sequence E description binding site for residue URC A 1404 source : AC4 41) chain A residue 880 type sequence R description binding site for residue URC A 1404 source : AC4 42) chain A residue 914 type sequence F description binding site for residue URC A 1404 source : AC4 43) chain A residue 1008 type sequence S description binding site for residue URC A 1404 source : AC4 44) chain A residue 1009 type sequence F description binding site for residue URC A 1404 source : AC4 45) chain A residue 1010 type sequence T description binding site for residue URC A 1404 source : AC4 46) chain A residue 1078 type sequence A description binding site for residue URC A 1404 source : AC4 47) chain A residue 1079 type sequence A description binding site for residue URC A 1404 source : AC4 48) chain A residue 1261 type sequence E description binding site for residue URC A 1404 source : AC4 49) chain A residue 839 type sequence R description binding site for residue BCT A 1405 source : AC5 50) chain A residue 840 type sequence H description binding site for residue BCT A 1405 source : AC5 51) chain A residue 877 type sequence I description binding site for residue BCT A 1405 source : AC5 52) chain A residue 909 type sequence T description binding site for residue BCT A 1405 source : AC5 53) chain A residue 910 type sequence A description binding site for residue BCT A 1405 source : AC5 54) chain A residue 911 type sequence F description binding site for residue BCT A 1405 source : AC5 55) chain A residue 914 type sequence F description binding site for residue BCT A 1405 source : AC5 56) chain A residue 915 type sequence G description binding site for residue BCT A 1405 source : AC5 57) chain A residue 918 type sequence Q description binding site for residue BCT A 1405 source : AC5 58) chain A residue 867 type sequence G description binding site for residue CA A 1406 source : AC6 59) chain A residue 870 type sequence T description binding site for residue CA A 1406 source : AC6 60) chain A residue 871 type sequence E description binding site for residue CA A 1406 source : AC6 61) chain A residue 874 type sequence S description binding site for residue CA A 1406 source : AC6 62) chain A residue 907 type sequence S description binding site for residue CA A 1406 source : AC6 63) chain A residue 908 type sequence N description binding site for residue CA A 1406 source : AC6 64) chain A residue 740 type sequence E description binding site for residue CA A 1407 source : AC7 65) chain A residue 741 type sequence H description binding site for residue CA A 1407 source : AC7 66) chain A residue 743 type sequence Y description binding site for residue CA A 1407 source : AC7 67) chain A residue 836 type sequence T description binding site for residue CA A 1407 source : AC7 68) chain A residue 837 type sequence G description binding site for residue CA A 1407 source : AC7 69) chain A residue 43-51 type prosite sequence CGEGGCGAC description 2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CGEGGCGAC source prosite : PS00197 70) chain A residue 797-832 type prosite sequence GFGGKETRSTVVSTALALAAHKTGRPVRCMLDRDED description MOLYBDOPTERIN_EUK Eukaryotic molybdopterin oxidoreductases signature. GFggKetrstvvstala..LaahKTgrpVrCmlDRdeD source prosite : PS00559 71) chain A residue 1261 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI1 72) chain A residue 43 type BINDING sequence C description BINDING => ECO:0000269|PubMed:17301076, ECO:0007744|PDB:2E3T source Swiss-Prot : SWS_FT_FI2 73) chain A residue 48 type BINDING sequence C description BINDING => ECO:0000269|PubMed:17301076, ECO:0007744|PDB:2E3T source Swiss-Prot : SWS_FT_FI2 74) chain A residue 51 type BINDING sequence C description BINDING => ECO:0000269|PubMed:17301076, ECO:0007744|PDB:2E3T source Swiss-Prot : SWS_FT_FI2 75) chain A residue 73 type BINDING sequence C description BINDING => ECO:0000269|PubMed:17301076, ECO:0007744|PDB:2E3T source Swiss-Prot : SWS_FT_FI2 76) chain A residue 112 type BINDING sequence C description BINDING => ECO:0000269|PubMed:17301076, ECO:0007744|PDB:2E3T source Swiss-Prot : SWS_FT_FI2 77) chain A residue 115 type BINDING sequence C description BINDING => ECO:0000269|PubMed:17301076, ECO:0007744|PDB:2E3T source Swiss-Prot : SWS_FT_FI2 78) chain A residue 147 type BINDING sequence C description BINDING => ECO:0000269|PubMed:17301076, ECO:0007744|PDB:2E3T source Swiss-Prot : SWS_FT_FI2 79) chain A residue 149 type BINDING sequence C description BINDING => ECO:0000269|PubMed:17301076, ECO:0007744|PDB:2E3T source Swiss-Prot : SWS_FT_FI2 80) chain A residue 256 type BINDING sequence L description BINDING => ECO:0000269|PubMed:15878860, ECO:0000269|PubMed:17301076 source Swiss-Prot : SWS_FT_FI3 81) chain A residue 346 type BINDING sequence S description BINDING => ECO:0000269|PubMed:15878860, ECO:0000269|PubMed:17301076 source Swiss-Prot : SWS_FT_FI3 82) chain A residue 359 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15878860, ECO:0000269|PubMed:17301076 source Swiss-Prot : SWS_FT_FI3 83) chain A residue 403 type BINDING sequence L description BINDING => ECO:0000269|PubMed:15878860, ECO:0000269|PubMed:17301076 source Swiss-Prot : SWS_FT_FI3 84) chain A residue 336 type BINDING sequence F description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 85) chain A residue 421 type BINDING sequence K description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 86) chain A residue 767 type BINDING sequence Q description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 87) chain A residue 798 type BINDING sequence F description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 88) chain A residue 912 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 89) chain A residue 914 type BINDING sequence F description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 90) chain A residue 1079 type BINDING sequence A description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 91) chain A residue 802 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI5 92) chain A residue 880 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI5 93) chain A residue 1010 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI5

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