Structure of PDB 3nrz Chain C

Receptor sequence
>3nrzC (length=756) Species: 9913 (Bos taurus) [Search protein sequence]
DTVGRPLPHLAAAMQASGEAVYCDDIPRYENELFLRLVTSTRAHAKIKSI
DVSEAQKVPGFVCFLSADDIPGSNETGLFNDETVFAKDTVTCVGHIIGAV
VADTPEHAERAAHVVKVTYEDLPAIITIEDAIKNNSFYGSELKIEKGDLK
KGFSEADNVVSGELYIGGQDHFYLETHCTIAIPKGEEGEMELFVSTQNAM
KTQSFVAKMLGVPVNRILVRVKRMGGGFGGKETRSTLVSVAVALAAYKTG
HPVRCMLDRNEDMLITGGRHPFLARYKVGFMKTGTIVALEVDHYSNAGNS
RDLSHSIMERALFHMDNCYKIPNIRGTGRLCKTNLSSNTAFRGFGGPQAL
FIAENWMSEVAVTCGLPAEEVRWKNMYKEGDLTHFNQRLEGFSVPRCWDE
CLKSSQYYARKSEVDKFNKENCWKKRGLCIIPTKFGISFTVPFLNQAGAL
IHVYTDGSVLVSHGGTEMGQGLHTKMVQVASKALKIPISKIYISETSTNT
VPNSSPTAASVSTDIYGQAVYEACQTILKRLEPFKKKNPDGSWEDWVMAA
YQDRVSLSTTGFYRTPNLGYSFETNSGNAFHYFTYGVACSEVEIDCLTGD
HKNLRTDIVMDVGSSLNPAIDIGQVEGAFVQGLGLFTLEELHYSPEGSLH
TRGPSTYKIPAFGSIPTEFRVSLLRDCPNKKAIYASKAVGEPPLFLGASV
FFAIKDAIRAARAQHTNNNTKELFRLDSPATPEKIRNACVDKFTTLCVTG
APGNCK
3D structure
PDB3nrz Substrate orientation and catalytic specificity in the action of xanthine oxidase: the sequential hydroxylation of hypoxanthine to uric acid.
ChainC
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q767 E802 R880 H884 R912 G1260 E1261
Catalytic site (residue number reindexed from 1) Q197 E232 R310 H314 R342 G690 E691
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 HPA C E802 R880 F914 F1009 T1010 A1079 E232 R310 F344 F439 T440 A509 PDBbind-CN: -logKd/Ki=5.34,Kd=4.6uM
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0016491 oxidoreductase activity
GO:0043546 molybdopterin cofactor binding

View graph for
Molecular Function
External links
PDB RCSB:3nrz, PDBe:3nrz, PDBj:3nrz
PDBsum3nrz
PubMed20615869
UniProtP80457|XDH_BOVIN Xanthine dehydrogenase/oxidase (Gene Name=XDH)

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