Structure of PDB 3uni Chain A

Receptor sequence

>3uniA (length=1289) Species: 9913 (Bos taurus)

ADELVFFVNGKKVVEKNADPETTLLAYLRRKLGLRGTKLGCGEGGCGACT
VMLSKYDRLQDKIIHFSANACLAPICTLHHVAVTTVEGIGSTKTRLHPVQ
ERIAKSHGSQCGFCTPGIVMSMYTLLRNQPEPTVEEIEDAFQGNLCRCTG
YRPILQGFRTFAPSLFNPEEFMPLDPTQEPIFPPELLRLKDVPPKQLRFE
GERVTWIQASTLKELLDLKAQHPEAKLVVGNTEIGIEMKFKNQLFPMIIC
PAWIPELNAVEHGPEGISFGAACALSSVEKTLLEAVAKLPTQKTEVFRGV
LEQLRWFAGKQVKSVASLGGNIITASPISDLNPVFMASGTKLTIVSRGTR
RTVPMDHTFFPSYRKTLLGPEEILLSIEIPYSREDEFFSAFKQASRREDD
IAKVTCGMRVLFQPGSMQVKELALCYGGMADRTISALKTTQKQLSKFWNE
KLLQDVCAGLAEELSLSPDAPGGMIEFRRTLTLSFFFKFYLTVLKKLGLD
PTYTSATLLFQKDPPANIQLFQEVPNGQSKEDTVGRPLPHLAAAMQASGE
AVYCDDIPRYENELFLRLVTSTRAHAKIKSIDVSEAQKVPGFVCFLSADD
IPGSNETGLFNDETVFAKDTVTCVGHIIGAVVADTPEHAERAAHVVKVTY
EDLPAIITIEDAIKNNSFYGSELKIEKGDLKKGFSEADNVVSGELYIGGQ
DHFYLETHCTIAIPKGEEGEMELFVSTQNAMKTQSFVAKMLGVPVNRILV
RVKRMGGGFGGKETRSTLVSVAVALAAYKTGHPVRCMLDRNEDMLITGGR
HPFLARYKVGFMKTGTIVALEVDHYSNAGNSRDLSHSIMERALFHMDNCY
KIPNIRGTGRLCKTNLSSNTAFRGFGGPQALFIAENWMSEVAVTCGLPAE
EVRWKNMYKEGDLTHFNQRLEGFSVPRCWDECLKSSQYYARKSEVDKFNK
ENCWKKRGLCIIPTKFGISFTVPFLNQAGALIHVYTDGSVLVSHGGTEMG
QGLHTKMVQVASKALKIPISKIYISETSTNTVPNSSPTAASVSTDIYGQA
VYEACQTILKRLEPFKKKNPDGSWEDWVMAAYQDRVSLSTTGFYRTPNLG
YSFETNSGNAFHYFTYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPA
IDIGQVEGAFVQGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFGSIPTEF
RVSLLRDCPNKKAIYASKAVGEPPLFLGASVFFAIKDAIRAARAQHTNNN
TKELFRLDSPATPEKIRNACVDKFTTLCVTGAKPWSLRV

3D structure

• PDB: 3uni Protein conformational gating of enzymatic activity in xanthine oxidoreductase.
• Chain: A
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Q767 E802 R880 H884 R912 G1260 E1261
• Catalytic site (residue number reindexed from 1): Q728 E763 R841 H845 R873 G1221 E1222
• Enzyme Commision number: 1.17.1.4: xanthine dehydrogenase.
  1.17.3.2: xanthine oxidase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	FES	A	Q112 C113 G114 C116 C148 C150 L744	Q110 C111 G112 C114 C146 C148 L705
BS02	FES	A	G42 C43 G44 G46 C48 G49 C51 N71 C73	G40 C41 G42 G44 C46 G47 C49 N69 C71
BS03	FAD	A	E45 G46 L257 V258 V259 G260 N261 T262 E263 I264 F337 A338 V342 A346 S347 G350 N351 I353 T354 S359 D360 I403 L404 D429	E43 G44 L227 V228 V229 G230 N231 T232 E233 I234 F307 A308 V312 A316 S317 G320 N321 I323 T324 S329 D330 I373 L374 D399
BS04	NAI	A	E263 K271 P357 I358 Y393 R394 D430 I431 G458 A460 D461 P501 R508 S1225	E233 K241 P327 I328 Y363 R364 D400 I401 G428 A430 D431 P471 R478 S1186
BS05	CO3	A	R839 H840 T909 A910 F911 F914 G915 Q918	R800 H801 T870 A871 F872 F875 G876 Q879
BS06	CA	A	A867 S870 R871 S874 S907 N908	A828 S831 R832 S835 S868 N869

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

External links

• PDB: RCSB:3uni, PDBe:3uni, PDBj:3uni
• PDBsum: 3uni
• PubMed: 22145797
• UniProt: P80457|XDH_BOVIN Xanthine dehydrogenase/oxidase (Gene Name=XDH)