Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T40954 | Target Info | |||
| Target Name | Xanthine dehydrogenase/oxidase (XDH) | ||||
| Synonyms | Xanthine oxidase; Xanthine dehydrogenase; XDHA | ||||
| Target Type | Successful Target | ||||
| Gene Name | XDH | ||||
| Biochemical Class | CH/CH(2) oxidoreductase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Flavin-Adenine Dinucleotide | Ligand Info | |||
| Canonical SMILES | CC1=CC2=C(C=C1C)N(C3=NC(=O)NC(=O)C3=N2)CC(C(C(COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)N5C=NC6=C(N=CN=C65)N)O)O)O)O)O | ||||
| InChI | 1S/C27H33N9O15P2/c1-10-3-12-13(4-11(10)2)35(24-18(32-12)25(42)34-27(43)33-24)5-14(37)19(39)15(38)6-48-52(44,45)51-53(46,47)49-7-16-20(40)21(41)26(50-16)36-9-31-17-22(28)29-8-30-23(17)36/h3-4,8-9,14-16,19-21,26,37-41H,5-7H2,1-2H3,(H,44,45)(H,46,47)(H2,28,29,30)(H,34,42,43)/t14-,15+,16+,19-,20+,21+,26+/m0/s1 | ||||
| InChIKey | VWWQXMAJTJZDQX-UYBVJOGSSA-N | ||||
| PubChem Compound ID | 643975 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 2E1Q Crystal Structure of Human Xanthine Oxidoreductase mutant, Glu803Val | ||||||
| Method | X-ray diffraction | Resolution | 2.60 Å | Mutation | Yes | [1] |
| PDB Sequence |
ADKLVFFVNG
12 RKVVEKNADP22 ETTLLAYLRR32 KLGLSGTKLG42 CGEGGCGACT52 VMLSKYDRLQ 62 NKIVHFSANA72 CLAPICSLHH82 VAVTTVEGIG92 STKTRLHPVQ102 ERIAKSHGSQ 112 CGFCTPGIVM122 SMYTLLRNQP132 EPTMEEIENA142 FQGNLCRCTG152 YRPILQGFRT 162 FARDGSPSLF196 KPEEFTPLDP206 TQEPIFPPEL216 LRLKDTPRKQ226 LRFEGERVTW 236 IQASTLKELL246 DLKAQHPDAK256 LVVGNTEIGI266 EMKFKNMLFP276 MIVCPAWIPE 286 LNSVEHGPDG296 ISFGAACPLS306 IVEKTLVDAV316 AKLPAQKTEV326 FRGVLEQLRW 336 FAGKQVKSVA346 SVGGNIITAS356 PISDLNPVFM366 ASGAKLTLVS376 RGTRRTVQMD 386 HTFFPGYRKT396 LLSPEEILLS406 IEIPYSREGE416 YFSAFKQASR426 REDDIAKVTS 436 GMRVLFKPGT446 TEVQELALCY456 GGMANRTISA466 LKTTQRQLSK476 LWKEELLQDV 486 CAGLAEELHL496 PPDAPGGMVD506 FRCTLTLSFF516 FKFYLTVLQK526 LGQENLEDKC 536 GKLDPTFASA546 TLLFQKDPPA556 DVQLFQEVPK566 GQSEEDMVGR576 PLPHLAADMQ 586 ASGEAVYCDD596 IPRYENELSL606 RLVTSTRAHA616 KIKSIDTSEA626 KKVPGFVCFI 636 SADDVPGSNI646 TGICNDETVF656 AKDKVTCVGH666 IIGAVVADTP676 EHTQRAAQGV 686 KITYEELPAI696 ITIEDAIKNN706 SFYGPELKIE716 KGDLKKGFSE726 ADNVVSGEIY 736 IGGQEHFYLE746 THCTIAVPKG756 EAGEMELFVS766 TQNTMKTQSF776 VAKMLGVPAN 786 RIVVRVKRMG796 GGFGGKVTRS806 TVVSTAVALA816 AYKTGRPVRC826 MLDRDEDMLI 836 TGGRHPFLAR846 YKVGFMKTGT856 VVALEVDHFS866 NVGNTQDLSQ876 SIMERALFHM 886 DNCYKIPNIR896 GTGRLCKTNL906 PSNTAFRGFG916 GPQGMLIAEC926 WMSEVAVTCG 936 MPAEEVRRKN946 LYKEGDLTHF956 NQKLEGFTLP966 RCWEECLASS976 QYHARKSEVD 986 KFNKENCWKK996 RGLCIIPTKF1006 GISFTVPFLN1016 QAGALLHVYT1026 DGSVLLTHGG 1036 TEMGQGLHTK1046 MVQVASRALK1056 IPTSKIYISE1066 TSTNTVPNTS1076 PTAASVSADL 1086 NGQAVYAACQ1096 TILKRLEPYK1106 KKNPSGSWED1116 WVTAAYMDTV1126 SLSATGFYRT 1136 PNLGYSFETN1146 SGNPFHYFSY1156 GVACSEVEID1166 CLTGDHKNLR1176 TDIVMDVGSS 1186 LNPAIDIGQV1196 EGAFVQGLGL1206 FTLEELHYSP1216 EGSLHTRGPS1226 TYKIPAFGSI 1236 PIEFRVSLLR1246 DCPNKKAIYA1256 SKAVGEPPLF1266 LAASIFFAIK1276 DAIRAARAQH 1286 TGNNVKELFR1296 LDSPATPEKI1306 RNACVDKFTT1316 LCVTGVPENC1326 KPWSVRV |
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|
GLU45
3.478
GLY46
2.959
GLY47
3.816
LEU74
3.733
LYS256
3.220
LEU257
2.805
VAL258
3.418
VAL259
2.673
GLY260
2.972
ASN261
2.844
THR262
2.557
GLU263
2.987
ILE264
2.940
GLY265
4.765
ILE266
4.232
GLU267
4.949
LEU287
4.456
ALA301
3.892
LEU305
4.148
TRP336
3.933
PHE337
3.199
ALA338
3.403
|
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| PDB ID: 2CKJ Human milk xanthine oxidoreductase | ||||||
| Method | X-ray diffraction | Resolution | 3.59 Å | Mutation | No | [2] |
| PDB Sequence |
ADKLVFFVNG
12 RKVVEKNADP22 ETTLLAYLRR32 KLGLSGTKLG42 CGEGGCGACT52 VMLSKYDRLQ 62 NKIVHFSANA72 CLAPICSLHH82 VAVTTVEGIG92 STKTRLHPVQ102 ERIAKSHGSQ 112 CGFCTPGIVM122 SMYTLLRNQP132 EPTMEEIENA142 FQGNLCRCTG152 YRPILQGFRT 162 FARPSLFKPE199 EFTPLDPTQE209 PIFPPELLRL219 KDTPRKQLRF229 EGERVTWIQA 239 STLKELLDLK249 AQHPDAKLVV259 GNTEIGIEMK269 FKNMLFPMIV279 CPAWIPELNS 289 VEHGPDGISF299 GAACPLSIVE309 KTLVDAVAKL319 PAQKTEVFRG329 VLEQLRWFAG 339 KQVKSVASVG349 GNIITASPIS359 DLNPVFMASG369 AKLTLVSRGT379 RRTVQMDHTF 389 FPGYRKTLLS399 PEEILLSIEI409 PYSREGEYFS419 AFKQASDIAK433 VTSGMRVLFK 443 PGTTEVQELA453 LCYGGMANRT463 ISALKTTQRQ473 LSKLWKEELL483 QDVCAGLAEE 493 LHLPPDAPGG503 MVDFRCTLTL513 SFFFKFYLTV523 LQKLGQENLE533 VQLFQEVPKG 567 QSEEDMVGRP577 LPHLAADMQA587 SGEAVYCDDI597 PRYENELSLR607 LVTSTRAHAK 617 IKSIDTSEAK627 KVPGFVCFIS637 ADDVPGSNIT647 GICNDETVFA657 KDKVTCVGHI 667 IGAVVADTPE677 HTQRAAQGVK687 ITYEELPAII697 TIEDAIKNNS707 FYGPELKIEK 717 GDLKKGFSEA727 DNVVSGEIYI737 GGQEHFYLET747 HCTIAVPKGE757 AGEMELFVST 767 QNTMKTQSFV777 AKMLGVPANR787 IVVRVKRMGG797 GFGGKETRST807 VVSTAVALAA 817 YKTGRPVRCM827 LDRDEDMLIT837 GGRHPFLARY847 KVGFMKTGTV857 VALEVDHFSN 867 VGNTQDLSQS877 IMERALFHMD887 NCYKIPNIRG897 TGRLCKTNLP907 SNTAFRGFGG 917 PQGMLIAECW927 MSEVAVTCGM937 PAEEVRRKNL947 YKEGDLTHFN957 QKLEGFTLPR 967 CWEECLASSQ977 YHARKSEVDK987 FNKENCWKKR997 GLCIIPTKFG1007 ISFTVPFLNQ 1017 AGALLHVYTD1027 GSVLLTHGGT1037 EMGQGLHTKM1047 VQVASRALKI1057 PTSKIYISET 1067 STNTVPNTSP1077 TAASVSADLN1087 GQAVYAACQT1097 ILKRLEPYKK1107 KNPSGSWEDW 1117 VTAAYMDTVS1127 LSATGFYRTP1137 NLGYSFETNS1147 GNPFHYFSYG1157 VACSEVEIDC 1167 LTGDHKNLRT1177 DIVMDVGSSL1187 NPAIDIGQVE1197 GAFVQGLGLF1207 TLEELHYSPE 1217 GSLHTRGPST1227 YKIPAFGSIP1237 IEFRVSLLRD1247 CPNKKAIYAS1257 KAVGEPPLFL 1267 AASIFFAIKD1277 AIRAARAQHT1287 GNNVKELFRL1297 DSPATPEKIR1307 NACVDKFTTL 1317 CVTW
|
|||||
|
|
GLU45
4.000
GLY46
3.671
GLY47
3.942
LYS256
3.558
LEU257
2.941
VAL258
3.480
VAL259
2.901
GLY260
2.485
ASN261
3.007
THR262
2.547
GLU263
2.908
ILE264
3.614
ILE266
4.677
ALA301
3.881
LEU305
4.378
TRP336
4.428
PHE337
2.958
ALA338
3.536
|
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Human xanthine oxidase changes its substrate specificity to aldehyde oxidase type upon mutation of amino acid residues in the active site: roles of active site residues in binding and activation of purine substrate. J Biochem. 2007 Apr;141(4):513-24. | ||||
| REF 2 | Human Milk Xanthine Dehydrogenase is Incompletely Converted to the Oxidase Form in the Absence of Proteolysis. A Structural Explanation. | ||||
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