eF-site ID 1fiq-ABC PDB Code 1fiq Chain A, B, C click to enlarge Title CRYSTAL STRUCTURE OF XANTHINE OXIDASE FROM BOVINE MILK Classification OXIDOREDUCTASE Compound XANTHINE OXIDASE Source ORGANISM_COMMON: cattle; ORGANISM_SCIENTIFIC: Bos taurus; Sequence A:  TADELVFFVNGKKVVEKNADPETTLLAYLRRKLGLRGTKL GCGEGGCGACTVMLSKYDRLQDKIIHFSANACLAPICTLH HVAVTTVEGIGSTKTRLHPVQERIAKSHGSQCGFCTPGIV MSMYTLLRNQPEPTVEEIEDAFQGNLCRCTGYRPILQGFR TFAK B:  PKQLRFEGERVTWIQASTLKELLDLKAQHPEAKLVVGNTE IGIEMKFKNQLFPMIICPAWIPELNAVEHGPEGISFGAAC ALSSVEKTLLEAVAKLPTQKTEVFRGVLEQLRWFAGKQVK SVASLGGNIITASPISDLNPVFMASGTKLTIVSRGTRRTV PMDHTFFPSYRKTLLGPEEILLSIEIPYSREDEFFSAFKQ ASRREDDIAKVTCGMRVLFQPGSMQVKELALCYGGMADRT ISALKTTQKQLSKFWNEKLLQDVCAGLAEELSLSPDAPGG MIEFRRTLTLSFFFKFYLTVLKKLG C:  DTVGRPLPHLAAAMQASGEAVYCDDIPRYENELFLRLVTS TRAHAKIKSIDVSEAQKVPGFVCFLSADDIPGSNETGLFN DETVFAKDTVTCVGHIIGAVVADTPEHAERAAHVVKVTYE DLPAIITIEDAIKNNSFYGSELKIEKGDLKKGFSEADNVV SGELYIGGQDHFYLETHCTIAIPKGEEGEMELFVSTQNAM KTQSFVAKMLGVPVNRILVRVKRMGGGFGGKETRSTLVSV AVALAAYKTGHPVRCMLDRNEDMLITGGRHPFLARYKVGF MKTGTIVALEVDHYSNAGNSRDLSHSIMERALFHMDNCYK IPNIRGTGRLCKTNLSSNTAFRGFGGPQALFIAENWMSEV AVTCGLPAEEVRWKNMYKEGDLTHFNQRLEGFSVPRCWDE CLKSSQYYARKSEVDKFNKENCWKKRGLCIIPTKFGISFT VPFLNQAGALIHVYTDGSVLVSHGGTEMGQGLHTKMVQVA SKALKIPISKIYISETSTNTVPNSSPTAASVSTDIYGQAV YEACQTILKRLEPFKKKNPDGSWEDWVMAAYQDRVSLSTT GFYRTPNLGYSFETNSGNAFHYFTYGVACSEVEIDCLTGD HKNLRTDIVMDVGSSLNPAIDIGQVEGAFVQGLGLFTLEE LHYSPEGSLHTRGPSTYKIPAFGSIPTEFRVSLLRDCPNK KAIYASKAVGEPPLFLGASVFFAIKDAIRAARAQHTNNNT KELFRLDSPATPEKIRNACVDKFTT Description Functional site 1) chain A residue 112 type sequence Q description BINDING SITE FOR RESIDUE FES A 601 source : AC1 2) chain A residue 113 type sequence C description BINDING SITE FOR RESIDUE FES A 601 source : AC1 3) chain A residue 114 type sequence G description BINDING SITE FOR RESIDUE FES A 601 source : AC1 4) chain A residue 116 type sequence C description BINDING SITE FOR RESIDUE FES A 601 source : AC1 5) chain A residue 148 type sequence C description BINDING SITE FOR RESIDUE FES A 601 source : AC1 6) chain A residue 149 type sequence R description BINDING SITE FOR RESIDUE FES A 601 source : AC1 7) chain A residue 150 type sequence C description BINDING SITE FOR RESIDUE FES A 601 source : AC1 8) chain A residue 42 type sequence G description BINDING SITE FOR RESIDUE FES A 602 source : AC2 9) chain A residue 43 type sequence C description BINDING SITE FOR RESIDUE FES A 602 source : AC2 10) chain A residue 44 type sequence G description BINDING SITE FOR RESIDUE FES A 602 source : AC2 11) chain A residue 46 type sequence G description BINDING SITE FOR RESIDUE FES A 602 source : AC2 12) chain A residue 47 type sequence G description BINDING SITE FOR RESIDUE FES A 602 source : AC2 13) chain A residue 48 type sequence C description BINDING SITE FOR RESIDUE FES A 602 source : AC2 14) chain A residue 49 type sequence G description BINDING SITE FOR RESIDUE FES A 602 source : AC2 15) chain A residue 51 type sequence C description BINDING SITE FOR RESIDUE FES A 602 source : AC2 16) chain A residue 71 type sequence N description BINDING SITE FOR RESIDUE FES A 602 source : AC2 17) chain A residue 73 type sequence C description BINDING SITE FOR RESIDUE FES A 602 source : AC2 18) chain A residue 112 type sequence Q description BINDING SITE FOR RESIDUE MTE C 1333 source : AC3 19) chain A residue 150 type sequence C description BINDING SITE FOR RESIDUE MTE C 1333 source : AC3 20) chain C residue 796 type sequence G description BINDING SITE FOR RESIDUE MTE C 1333 source : AC3 21) chain C residue 797 type sequence G description BINDING SITE FOR RESIDUE MTE C 1333 source : AC3 22) chain C residue 798 type sequence F description BINDING SITE FOR RESIDUE MTE C 1333 source : AC3 23) chain C residue 912 type sequence R description BINDING SITE FOR RESIDUE MTE C 1333 source : AC3 24) chain C residue 1038 type sequence M description BINDING SITE FOR RESIDUE MTE C 1333 source : AC3 25) chain C residue 1039 type sequence G description BINDING SITE FOR RESIDUE MTE C 1333 source : AC3 26) chain C residue 1040 type sequence Q description BINDING SITE FOR RESIDUE MTE C 1333 source : AC3 27) chain C residue 1078 type sequence A description BINDING SITE FOR RESIDUE MTE C 1333 source : AC3 28) chain C residue 1079 type sequence A description BINDING SITE FOR RESIDUE MTE C 1333 source : AC3 29) chain C residue 1080 type sequence S description BINDING SITE FOR RESIDUE MTE C 1333 source : AC3 30) chain C residue 1081 type sequence V description BINDING SITE FOR RESIDUE MTE C 1333 source : AC3 31) chain C residue 1082 type sequence S description BINDING SITE FOR RESIDUE MTE C 1333 source : AC3 32) chain C residue 1194 type sequence Q description BINDING SITE FOR RESIDUE MTE C 1333 source : AC3 33) chain C residue 1261 type sequence E description BINDING SITE FOR RESIDUE MTE C 1333 source : AC3 34) chain C residue 767 type sequence Q description BINDING SITE FOR RESIDUE MOS C 1334 source : AC4 35) chain C residue 798 type sequence F description BINDING SITE FOR RESIDUE MOS C 1334 source : AC4 36) chain C residue 799 type sequence G description BINDING SITE FOR RESIDUE MOS C 1334 source : AC4 37) chain C residue 911 type sequence F description BINDING SITE FOR RESIDUE MOS C 1334 source : AC4 38) chain C residue 912 type sequence R description BINDING SITE FOR RESIDUE MOS C 1334 source : AC4 39) chain C residue 1078 type sequence A description BINDING SITE FOR RESIDUE MOS C 1334 source : AC4 40) chain C residue 1079 type sequence A description BINDING SITE FOR RESIDUE MOS C 1334 source : AC4 41) chain C residue 1261 type sequence E description BINDING SITE FOR RESIDUE MOS C 1334 source : AC4 42) chain C residue 802 type sequence E description BINDING SITE FOR RESIDUE SAL C 1335 source : AC5 43) chain C residue 880 type sequence R description BINDING SITE FOR RESIDUE SAL C 1335 source : AC5 44) chain C residue 914 type sequence F description BINDING SITE FOR RESIDUE SAL C 1335 source : AC5 45) chain C residue 1008 type sequence S description BINDING SITE FOR RESIDUE SAL C 1335 source : AC5 46) chain C residue 1009 type sequence F description BINDING SITE FOR RESIDUE SAL C 1335 source : AC5 47) chain C residue 1010 type sequence T description BINDING SITE FOR RESIDUE SAL C 1335 source : AC5 48) chain C residue 1011 type sequence V description BINDING SITE FOR RESIDUE SAL C 1335 source : AC5 49) chain A residue 45 type sequence E description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 50) chain A residue 46 type sequence G description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 51) chain B residue 256 type sequence K description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 52) chain B residue 257 type sequence L description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 53) chain B residue 258 type sequence V description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 54) chain B residue 259 type sequence V description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 55) chain B residue 260 type sequence G description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 56) chain B residue 261 type sequence N description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 57) chain B residue 262 type sequence T description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 58) chain B residue 263 type sequence E description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 59) chain B residue 264 type sequence I description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 60) chain B residue 287 type sequence L description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 61) chain B residue 337 type sequence F description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 62) chain B residue 338 type sequence A description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 63) chain B residue 346 type sequence A description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 64) chain B residue 347 type sequence S description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 65) chain B residue 350 type sequence G description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 66) chain B residue 351 type sequence N description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 67) chain B residue 353 type sequence I description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 68) chain B residue 354 type sequence T description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 69) chain B residue 359 type sequence S description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 70) chain B residue 360 type sequence D description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 71) chain B residue 404 type sequence L description BINDING SITE FOR RESIDUE FAD B 606 source : AC6 72) chain C residue 839 type sequence R description BINDING SITE FOR RESIDUE GOL C 1336 source : AC7 73) chain C residue 840 type sequence H description BINDING SITE FOR RESIDUE GOL C 1336 source : AC7 74) chain C residue 877 type sequence I description BINDING SITE FOR RESIDUE GOL C 1336 source : AC7 75) chain C residue 909 type sequence T description BINDING SITE FOR RESIDUE GOL C 1336 source : AC7 76) chain C residue 910 type sequence A description BINDING SITE FOR RESIDUE GOL C 1336 source : AC7 77) chain C residue 911 type sequence F description BINDING SITE FOR RESIDUE GOL C 1336 source : AC7 78) chain C residue 914 type sequence F description BINDING SITE FOR RESIDUE GOL C 1336 source : AC7 79) chain C residue 915 type sequence G description BINDING SITE FOR RESIDUE GOL C 1336 source : AC7 80) chain C residue 918 type sequence Q description BINDING SITE FOR RESIDUE GOL C 1336 source : AC7 81) chain C residue 803 type catalytic sequence T description 139 source MCSA : MCSA1 82) chain C residue 881 type catalytic sequence A description 139 source MCSA : MCSA1 83) chain C residue 1262 type catalytic sequence P description 139 source MCSA : MCSA1 84) 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 85) chain C residue 797-832 type prosite sequence GFGGKETRSTLVSVAVALAAYKTGHPVRCMLDRNED description MOLYBDOPTERIN_EUK Eukaryotic molybdopterin oxidoreductases signature. GFggKetrstlvsvava..LaayKTghpVrCmlDRneD source prosite : PS00559 86) chain C residue 1262 type ACT_SITE sequence P description Proton acceptor => ECO:0000269|PubMed:15148401 source Swiss-Prot : SWS_FT_FI1 87) chain B residue 338 type ACT_SITE sequence A description Proton acceptor => ECO:0000269|PubMed:15148401 source Swiss-Prot : SWS_FT_FI1 88) chain B residue 348 type ACT_SITE sequence L description Proton acceptor => ECO:0000269|PubMed:15148401 source Swiss-Prot : SWS_FT_FI1 89) chain B residue 361 type ACT_SITE sequence L description Proton acceptor => ECO:0000269|PubMed:15148401 source Swiss-Prot : SWS_FT_FI1 90) chain B residue 405 type ACT_SITE sequence L description Proton acceptor => ECO:0000269|PubMed:15148401 source Swiss-Prot : SWS_FT_FI1 91) chain B residue 423 type ACT_SITE sequence Q description Proton acceptor => ECO:0000269|PubMed:15148401 source Swiss-Prot : SWS_FT_FI1 92) chain A residue 148 type ACT_SITE sequence C description Proton acceptor => ECO:0000269|PubMed:15148401 source Swiss-Prot : SWS_FT_FI1 93) chain A residue 150 type ACT_SITE sequence C description Proton acceptor => ECO:0000269|PubMed:15148401 source Swiss-Prot : SWS_FT_FI1 94) chain C residue 768 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252 source Swiss-Prot : SWS_FT_FI2 95) chain C residue 799 type BINDING sequence G description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252 source Swiss-Prot : SWS_FT_FI2 96) chain C residue 913 type BINDING sequence G description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252 source Swiss-Prot : SWS_FT_FI2 97) chain C residue 1080 type BINDING sequence S description BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252 source Swiss-Prot : SWS_FT_FI2 98) chain C residue 803 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI3 99) chain C residue 881 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI3 100) chain C residue 915 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI3 101) chain C residue 1011 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI3

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