Online Services

●I-TASSER ●I-TASSER-MTD ●C-I-TASSER ●CR-I-TASSER ●QUARK ●C-QUARK ●LOMETS ●MUSTER ●CEthreader ●SEGMER ●DeepFold ●DeepFoldRNA ●FoldDesign ●COFACTOR ●COACH ●MetaGO ●TripletGO ●IonCom ●FG-MD ●ModRefiner ●REMO ●DEMO ●DEMO-EM ●SPRING ●COTH ●Threpp ●PEPPI ●BSpred ●ANGLOR ●EDock ●BSP-SLIM ●SAXSTER ●FUpred ●ThreaDom ●ThreaDomEx ●EvoDesign ●BindProf ●BindProfX ●SSIPe ●GPCR-I-TASSER ●MAGELLAN ●ResQ ●STRUM ●DAMpred

●TM-score ●TM-align ●US-align ●MM-align ●RNA-align ●NW-align ●LS-align ●EDTSurf ●MVP ●MVP-Fit ●SPICKER ●HAAD ●PSSpred ●3DRobot ●MR-REX ●I-TASSER-MR ●SVMSEQ ●NeBcon ●ResPRE ●TripletRes ●DeepPotential ●WDL-RF ●ATPbind ●DockRMSD ●DeepMSA ●FASPR ●EM-Refiner ●GPU-I-TASSER

●BioLiP ●E. coli ●GLASS ●GPCR-HGmod ●GPCR-RD ●GPCR-EXP ●Tara-3D ●TM-fold ●DECOYS ●POTENTIAL ●RW/RWplus ●EvoEF ●HPSF ●THE-DB ●ADDRESS ●Alpaca-Antibody ●CASP7 ●CASP8 ●CASP9 ●CASP10 ●CASP11 ●CASP12 ●CASP13 ●CASP14

Structure of PDB 1fo4 Chain A Binding Site BS02

Receptor Information >1fo4 Chain A (length=1299) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure] ADELVFFVNGKKVVEKNADPETTLLAYLRRKLGLRGTKLGCGEGGCGACT VMLSKYDRLQDKIIHFSANACLAPICTLHHVAVTTVEGIGSTKTRLHPVQ ERIAKSHGSQCGFCTPGIVMSMYTLLRNQPEPTVEEIEDAFQGNLCRCTG YRPILQGFRTFAKSPSLFNPEEFMPLDPTQEPIFPPELLRLKDVPPKQLR FEGERVTWIQASTLKELLDLKAQHPEAKLVVGNTEIGIEMKFKNQLFPMI ICPAWIPELNAVEHGPEGISFGAACALSSVEKTLLEAVAKLPTQKTEVFR GVLEQLRWFAGKQVKSVASLGGNIITASPISDLNPVFMASGTKLTIVSRG TRRTVPMDHTFFPSYRKTLLGPEEILLSIEIPYSREDEFFSAFKQASRRE DDIAKVTCGMRVLFQPGSMQVKELALCYGGMADRTISALKTTQKQLSKFW NEKLLQDVCAGLAEELSLSPDAPGGMIEFRRTLTLSFFFKFYLTVLKKLG KDSKLDPTYTSATLLFQKHPPANIQLFQEVPNGQSKEDTVGRPLPHLAAA MQASGEAVYCDDIPRYENELFLRLVTSTRAHAKIKSIDVSEAQKVPGFVC FLSADDIPGSNETGLFNDETVFAKDTVTCVGHIIGAVVADTPEHAERAAH VVKVTYEDLPAIITIEDAIKNNSFYGSELKIEKGDLKKGFSEADNVVSGE LYIGGQDHFYLETHCTIAIPKGEEGEMELFVSTQNAMKTQSFVAKMLGVP VNRILVRVKRMGGGFGGKETRSTLVSVAVALAAYKTGHPVRCMLDRNEDM LITGGRHPFLARYKVGFMKTGTIVALEVDHYSNAGNSRDLSHSIMERALF HMDNCYKIPNIRGTGRLCKTNLSSNTAFRGFGGPQALFIAENWMSEVAVT CGLPAEEVRWKNMYKEGDLTHFNQRLEGFSVPRCWDECLKSSQYYARKSE VDKFNKENCWKKRGLCIIPTKFGISFTVPFLNQAGALIHVYTDGSVLVSH GGTEMGQGLHTKMVQVASKALKIPISKIYISETSTNTVPNSSPTAASVST DIYGQAVYEACQTILKRLEPFKKKNPDGSWEDWVMAAYQDRVSLSTTGFY RTPNLGYSFETNSGNAFHYFTYGVACSEVEIDCLTGDHKNLRTDIVMDVG SSLNPAIDIGQVEGAFVQGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFG SIPTEFRVSLLRDCPNKKAIYASKAVGEPPLFLGASVFFAIKDAIRAARA QHTNNNTKELFRLDSPATPEKIRNACVDKFTTLCVTGAPGNCKPWSLRV

Ligand information Ligand ID FES InChI InChI=1S/2Fe.2S InChIKey NIXDOXVAJZFRNF-UHFFFAOYSA-N SMILES Software SMILES ACDLabs 10.04 [Fe]1S[Fe]S1 CACTVS 3.341 OpenEye OEToolkits 1.5.0 S1[Fe]S[Fe]1 Formula Fe2 S2 Name FE2/S2 (INORGANIC) CLUSTER ChEMBL DrugBank ZINC PDB chain 1fo4 Chain A Residue 3001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure Global view Local view Structure summary [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] PDB 1fo4 Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion. Resolution 2.1 Å Binding residue (original residue number in PDB) Q112 C113 G114 C116 C148 R149 C150 L744 Binding residue (residue number reindexed from 1) Q110 C111 G112 C114 C146 R147 C148 L711 Annotation score 1

Enzymatic activity Catalytic site (original residue number in PDB) Q767 E802 R880 H884 R912 G1260 E1261 Catalytic site (residue number reindexed from 1) Q734 E769 R847 H851 R879 G1227 E1228 Enzyme Commision number 1.17.1.4: xanthine dehydrogenase. 1.17.3.2: xanthine oxidase.

Gene Ontology Molecular Function GO:0004854 xanthine dehydrogenase activity GO:0004855 xanthine oxidase activity GO:0005506 iron ion binding GO:0016491 oxidoreductase activity GO:0030151 molybdenum ion binding GO:0042803 protein homodimerization activity GO:0043546 molybdopterin cofactor binding GO:0046872 metal ion binding GO:0050660 flavin adenine dinucleotide binding GO:0051536 iron-sulfur cluster binding GO:0051537 2 iron, 2 sulfur cluster binding GO:0071949 FAD binding

	Biological Process
GO:0009115	xanthine catabolic process

	Cellular Component
GO:0002197	xanthine dehydrogenase complex
GO:0005576	extracellular region
GO:0005615	extracellular space
GO:0005737	cytoplasm
GO:0005777	peroxisome

View graph for Molecular Function

View graph for Biological Process

View graph for Cellular Component