eF-site ID 1fo4-A PDB Code 1fo4 Chain A click to enlarge Title CRYSTAL STRUCTURE OF XANTHINE DEHYDROGENASE ISOLATED FROM BOVINE MILK Classification OXIDOREDUCTASE Compound XANTHINE DEHYDROGENASE Source ORGANISM_COMMON: cattle; ORGANISM_SCIENTIFIC: Bos taurus; Sequence A:  ADELVFFVNGKKVVEKNADPETTLLAYLRRKLGLRGTKLG CGEGGCGACTVMLSKYDRLQDKIIHFSANACLAPICTLHH VAVTTVEGIGSTKTRLHPVQERIAKSHGSQCGFCTPGIVM SMYTLLRNQPEPTVEEIEDAFQGNLCRCTGYRPILQGFRT FAKSPSLFNPEEFMPLDPTQEPIFPPELLRLKDVPPKQLR FEGERVTWIQASTLKELLDLKAQHPEAKLVVGNTEIGIEM KFKNQLFPMIICPAWIPELNAVEHGPEGISFGAACALSSV EKTLLEAVAKLPTQKTEVFRGVLEQLRWFAGKQVKSVASL GGNIITASPISDLNPVFMASGTKLTIVSRGTRRTVPMDHT FFPSYRKTLLGPEEILLSIEIPYSREDEFFSAFKQASRRE DDIAKVTCGMRVLFQPGSMQVKELALCYGGMADRTISALK TTQKQLSKFWNEKLLQDVCAGLAEELSLSPDAPGGMIEFR RTLTLSFFFKFYLTVLKKLGKDSKLDPTYTSATLLFQKHP PANIQLFQEVPNGQSKEDTVGRPLPHLAAAMQASGEAVYC DDIPRYENELFLRLVTSTRAHAKIKSIDVSEAQKVPGFVC FLSADDIPGSNETGLFNDETVFAKDTVTCVGHIIGAVVAD TPEHAERAAHVVKVTYEDLPAIITIEDAIKNNSFYGSELK IEKGDLKKGFSEADNVVSGELYIGGQDHFYLETHCTIAIP KGEEGEMELFVSTQNAMKTQSFVAKMLGVPVNRILVRVKR MGGGFGGKETRSTLVSVAVALAAYKTGHPVRCMLDRNEDM LITGGRHPFLARYKVGFMKTGTIVALEVDHYSNAGNSRDL SHSIMERALFHMDNCYKIPNIRGTGRLCKTNLSSNTAFRG FGGPQALFIAENWMSEVAVTCGLPAEEVRWKNMYKEGDLT HFNQRLEGFSVPRCWDECLKSSQYYARKSEVDKFNKENCW KKRGLCIIPTKFGISFTVPFLNQAGALIHVYTDGSVLVSH GGTEMGQGLHTKMVQVASKALKIPISKIYISETSTNTVPN SSPTAASVSTDIYGQAVYEACQTILKRLEPFKKKNPDGSW EDWVMAAYQDRVSLSTTGFYRTPNLGYSFETNSGNAFHYF TYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPAIDIG QVEGAFVQGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFG SIPTEFRVSLLRDCPNKKAIYASKAVGEPPLFLGASVFFA IKDAIRAARAQHTNNNTKELFRLDSPATPEKIRNACVDKF TTLCVTGAPGNCKPWSLRV Description Functional site 1) chain A residue 867 type sequence A description BINDING SITE FOR RESIDUE CA A 4009 source : AC1 2) chain A residue 870 type sequence S description BINDING SITE FOR RESIDUE CA A 4009 source : AC1 3) chain A residue 871 type sequence R description BINDING SITE FOR RESIDUE CA A 4009 source : AC1 4) chain A residue 874 type sequence S description BINDING SITE FOR RESIDUE CA A 4009 source : AC1 5) chain A residue 907 type sequence S description BINDING SITE FOR RESIDUE CA A 4009 source : AC1 6) chain A residue 908 type sequence N description BINDING SITE FOR RESIDUE CA A 4009 source : AC1 7) chain A residue 112 type sequence Q description BINDING SITE FOR RESIDUE FES A 3001 source : AC3 8) chain A residue 113 type sequence C description BINDING SITE FOR RESIDUE FES A 3001 source : AC3 9) chain A residue 114 type sequence G description BINDING SITE FOR RESIDUE FES A 3001 source : AC3 10) chain A residue 116 type sequence C description BINDING SITE FOR RESIDUE FES A 3001 source : AC3 11) chain A residue 148 type sequence C description BINDING SITE FOR RESIDUE FES A 3001 source : AC3 12) chain A residue 149 type sequence R description BINDING SITE FOR RESIDUE FES A 3001 source : AC3 13) chain A residue 150 type sequence C description BINDING SITE FOR RESIDUE FES A 3001 source : AC3 14) chain A residue 42 type sequence G description BINDING SITE FOR RESIDUE FES A 3002 source : AC4 15) chain A residue 43 type sequence C description BINDING SITE FOR RESIDUE FES A 3002 source : AC4 16) chain A residue 44 type sequence G description BINDING SITE FOR RESIDUE FES A 3002 source : AC4 17) chain A residue 46 type sequence G description BINDING SITE FOR RESIDUE FES A 3002 source : AC4 18) chain A residue 47 type sequence G description BINDING SITE FOR RESIDUE FES A 3002 source : AC4 19) chain A residue 48 type sequence C description BINDING SITE FOR RESIDUE FES A 3002 source : AC4 20) chain A residue 49 type sequence G description BINDING SITE FOR RESIDUE FES A 3002 source : AC4 21) chain A residue 51 type sequence C description BINDING SITE FOR RESIDUE FES A 3002 source : AC4 22) chain A residue 71 type sequence N description BINDING SITE FOR RESIDUE FES A 3002 source : AC4 23) chain A residue 73 type sequence C description BINDING SITE FOR RESIDUE FES A 3002 source : AC4 24) chain A residue 112 type sequence Q description BINDING SITE FOR RESIDUE MTE A 3003 source : AC5 25) chain A residue 150 type sequence C description BINDING SITE FOR RESIDUE MTE A 3003 source : AC5 26) chain A residue 796 type sequence G description BINDING SITE FOR RESIDUE MTE A 3003 source : AC5 27) chain A residue 797 type sequence G description BINDING SITE FOR RESIDUE MTE A 3003 source : AC5 28) chain A residue 798 type sequence F description BINDING SITE FOR RESIDUE MTE A 3003 source : AC5 29) chain A residue 912 type sequence R description BINDING SITE FOR RESIDUE MTE A 3003 source : AC5 30) chain A residue 1038 type sequence M description BINDING SITE FOR RESIDUE MTE A 3003 source : AC5 31) chain A residue 1039 type sequence G description BINDING SITE FOR RESIDUE MTE A 3003 source : AC5 32) chain A residue 1040 type sequence Q description BINDING SITE FOR RESIDUE MTE A 3003 source : AC5 33) chain A residue 1078 type sequence A description BINDING SITE FOR RESIDUE MTE A 3003 source : AC5 34) chain A residue 1079 type sequence A description BINDING SITE FOR RESIDUE MTE A 3003 source : AC5 35) chain A residue 1080 type sequence S description BINDING SITE FOR RESIDUE MTE A 3003 source : AC5 36) chain A residue 1081 type sequence V description BINDING SITE FOR RESIDUE MTE A 3003 source : AC5 37) chain A residue 1082 type sequence S description BINDING SITE FOR RESIDUE MTE A 3003 source : AC5 38) chain A residue 1194 type sequence Q description BINDING SITE FOR RESIDUE MTE A 3003 source : AC5 39) chain A residue 1261 type sequence E description BINDING SITE FOR RESIDUE MTE A 3003 source : AC5 40) chain A residue 767 type sequence Q description BINDING SITE FOR RESIDUE MOS A 3004 source : AC6 41) chain A residue 799 type sequence G description BINDING SITE FOR RESIDUE MOS A 3004 source : AC6 42) chain A residue 802 type sequence E description BINDING SITE FOR RESIDUE MOS A 3004 source : AC6 43) chain A residue 911 type sequence F description BINDING SITE FOR RESIDUE MOS A 3004 source : AC6 44) chain A residue 912 type sequence R description BINDING SITE FOR RESIDUE MOS A 3004 source : AC6 45) chain A residue 1078 type sequence A description BINDING SITE FOR RESIDUE MOS A 3004 source : AC6 46) chain A residue 1079 type sequence A description BINDING SITE FOR RESIDUE MOS A 3004 source : AC6 47) chain A residue 1261 type sequence E description BINDING SITE FOR RESIDUE MOS A 3004 source : AC6 48) chain A residue 802 type sequence E description BINDING SITE FOR RESIDUE SAL A 3005 source : AC7 49) chain A residue 880 type sequence R description BINDING SITE FOR RESIDUE SAL A 3005 source : AC7 50) chain A residue 914 type sequence F description BINDING SITE FOR RESIDUE SAL A 3005 source : AC7 51) chain A residue 1009 type sequence F description BINDING SITE FOR RESIDUE SAL A 3005 source : AC7 52) chain A residue 1010 type sequence T description BINDING SITE FOR RESIDUE SAL A 3005 source : AC7 53) chain A residue 1011 type sequence V description BINDING SITE FOR RESIDUE SAL A 3005 source : AC7 54) chain A residue 1079 type sequence A description BINDING SITE FOR RESIDUE SAL A 3005 source : AC7 55) chain A residue 45 type sequence E description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 56) chain A residue 46 type sequence G description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 57) chain A residue 47 type sequence G description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 58) chain A residue 74 type sequence L description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 59) chain A residue 256 type sequence K description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 60) chain A residue 257 type sequence L description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 61) chain A residue 258 type sequence V description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 62) chain A residue 259 type sequence V description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 63) chain A residue 260 type sequence G description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 64) chain A residue 261 type sequence N description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 65) chain A residue 262 type sequence T description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 66) chain A residue 263 type sequence E description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 67) chain A residue 264 type sequence I description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 68) chain A residue 301 type sequence A description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 69) chain A residue 337 type sequence F description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 70) chain A residue 338 type sequence A description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 71) chain A residue 342 type sequence V description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 72) chain A residue 346 type sequence A description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 73) chain A residue 347 type sequence S description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 74) chain A residue 350 type sequence G description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 75) chain A residue 351 type sequence N description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 76) chain A residue 353 type sequence I description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 77) chain A residue 354 type sequence T description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 78) chain A residue 359 type sequence S description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 79) chain A residue 360 type sequence D description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 80) chain A residue 403 type sequence I description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 81) chain A residue 404 type sequence L description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 82) chain A residue 422 type sequence K description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 83) chain A residue 429 type sequence D description BINDING SITE FOR RESIDUE FAD A 3006 source : AC8 84) chain A residue 839 type sequence R description BINDING SITE FOR RESIDUE GOL A 3007 source : BC6 85) chain A residue 840 type sequence H description BINDING SITE FOR RESIDUE GOL A 3007 source : BC6 86) chain A residue 877 type sequence I description BINDING SITE FOR RESIDUE GOL A 3007 source : BC6 87) chain A residue 909 type sequence T description BINDING SITE FOR RESIDUE GOL A 3007 source : BC6 88) chain A residue 910 type sequence A description BINDING SITE FOR RESIDUE GOL A 3007 source : BC6 89) chain A residue 911 type sequence F description BINDING SITE FOR RESIDUE GOL A 3007 source : BC6 90) chain A residue 913 type sequence G description BINDING SITE FOR RESIDUE GOL A 3007 source : BC6 91) chain A residue 914 type sequence F description BINDING SITE FOR RESIDUE GOL A 3007 source : BC6 92) chain A residue 915 type sequence G description BINDING SITE FOR RESIDUE GOL A 3007 source : BC6 93) chain A residue 918 type sequence Q description BINDING SITE FOR RESIDUE GOL A 3007 source : BC6 94) chain A residue 561 type sequence Q description BINDING SITE FOR RESIDUE GOL A 3008 source : BC7 95) chain A residue 574 type sequence G description BINDING SITE FOR RESIDUE GOL A 3008 source : BC7 96) chain A residue 1184 type sequence S description BINDING SITE FOR RESIDUE GOL A 3008 source : BC7 97) chain A residue 1185 type sequence S description BINDING SITE FOR RESIDUE GOL A 3008 source : BC7 98) chain A residue 802 type catalytic sequence E description 139 source MCSA : MCSA1 99) chain A residue 880 type catalytic sequence R description 139 source MCSA : MCSA1 100) chain A residue 1261 type catalytic sequence E description 139 source MCSA : MCSA1 101) 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 102) chain A residue 797-832 type prosite sequence GFGGKETRSTLVSVAVALAAYKTGHPVRCMLDRNED description MOLYBDOPTERIN_EUK Eukaryotic molybdopterin oxidoreductases signature. GFggKetrstlvsvava..LaayKTghpVrCmlDRneD source prosite : PS00559 103) chain A residue 1261 type ACT_SITE sequence E description Proton acceptor => ECO:0000269|PubMed:15148401 source Swiss-Prot : SWS_FT_FI1 104) chain A residue 43 type BINDING sequence C description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252 source Swiss-Prot : SWS_FT_FI2 105) chain A residue 798 type BINDING sequence F description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252 source Swiss-Prot : SWS_FT_FI2 106) chain A residue 912 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252 source Swiss-Prot : SWS_FT_FI2 107) chain A residue 1079 type BINDING sequence A description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252 source Swiss-Prot : SWS_FT_FI2 108) chain A residue 48 type BINDING sequence C description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252 source Swiss-Prot : SWS_FT_FI2 109) chain A residue 51 type BINDING sequence C description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252 source Swiss-Prot : SWS_FT_FI2 110) chain A residue 73 type BINDING sequence C description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252 source Swiss-Prot : SWS_FT_FI2 111) chain A residue 113 type BINDING sequence C description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252 source Swiss-Prot : SWS_FT_FI2 112) chain A residue 116 type BINDING sequence C description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252 source Swiss-Prot : SWS_FT_FI2 113) chain A residue 148 type BINDING sequence C description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252 source Swiss-Prot : SWS_FT_FI2 114) chain A residue 150 type BINDING sequence C description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252 source Swiss-Prot : SWS_FT_FI2 115) chain A residue 767 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252 source Swiss-Prot : SWS_FT_FI2 116) chain A residue 257 type BINDING sequence L description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401 source Swiss-Prot : SWS_FT_FI3 117) chain A residue 337 type BINDING sequence F description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401 source Swiss-Prot : SWS_FT_FI3 118) chain A residue 347 type BINDING sequence S description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401 source Swiss-Prot : SWS_FT_FI3 119) chain A residue 360 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401 source Swiss-Prot : SWS_FT_FI3 120) chain A residue 404 type BINDING sequence L description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401 source Swiss-Prot : SWS_FT_FI3 121) chain A residue 422 type BINDING sequence K description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401 source Swiss-Prot : SWS_FT_FI3 122) chain A residue 802 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI4 123) chain A residue 880 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI4 124) chain A residue 914 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI4 125) chain A residue 1010 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI4

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