Structure of PDB 3epx Chain B

Receptor sequence
>3epxB (length=324) Species: 5699 (Trypanosoma vivax) [Search protein sequence]
AKNVVLDHDGNLDDFVAMVLLASNTEKVRLIGALCTDADCFVENGFNVTG
KIMCLMHNNMNLPLFPIGKSAATAVNPFPKEWRCLAKNMDDMPILNIPEN
VELWDKIKAENEKYEGQQLLADLVMNSEEKVTICVTGPLSNVAWCIDKYG
EKFTSKVEECVIMGGAVDVRGNVFLPSTDGTAEWNIYWDPASAKTVFGCP
GLRRIMFSLDSTNTVPVRSPYVQRFGEQTNFLLSILVGTMWAMCTHCELL
RDGYYAWDALTAAYVVDQKVANVDPVPIDVVVDKQPNEGATVRTDAENYP
LTFVARNPEAEFFLDMLLRSARAC
3D structure
PDB3epx Crystal structures of T. vivax nucleoside hydrolase in complex with new potent and specific inhibitors.
ChainB
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D10 D15 D40 W83 T137 W185 N186 W260 D261
Catalytic site (residue number reindexed from 1) D9 D14 D39 W82 T136 W184 N185 W257 D258
Enzyme Commision number 3.2.2.1: purine nucleosidase.
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 CA B D10 D15 T137 D261 D9 D14 T136 D258
BS02 IMQ B N12 D14 D40 W83 M164 N173 E184 N186 Y257 W260 D261 N11 D13 D39 W82 M163 N172 E183 N185 Y254 W257 D258 MOAD: Ki=10.8nM
Gene Ontology
Molecular Function
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0016799 hydrolase activity, hydrolyzing N-glycosyl compounds
GO:0046872 metal ion binding
Biological Process
GO:0006139 nucleobase-containing compound metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3epx, PDBe:3epx, PDBj:3epx
PDBsum3epx
PubMed19281874
UniProtQ9GPQ4

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