Structure of PDB 4i72 Chain A

Receptor sequence
>4i72A (length=328) [Search protein sequence]
GSHMAKTVILDHDGNKDDFVAMILLLSNPKKVNLIGCICTDADCFVENGF
DVTGKIMCAMHRLIKTPLFPIGKSTATAVNAFPTEWRFSAKNLDDMPFLN
IVEDVALWEKLKPENEAHNGQQLLADLVMKSKEKVTVCVTGPLSNMAWCI
EKYGEAFTSKVEECVIMGGAVDVGGNVFLPTTDGSAEWNIYWDPPAAKKV
LCCPNIRCVLFSLDATNTVPVRSVDVKGFGAQNQYLLSQMVGTMWAMSTH
EEILRDGDAYYAWDALTAAYILEPTIATLEPVALDVDVSKGKSEGRTPRA
SGKPCVHVARNPSKQMFHDLVFASTRVC
3D structure
PDB4i72 Structures of purine nucleosidase from Trypanosoma brucei bound to isozyme-specific trypanocidals and a novel metalorganic inhibitor
ChainA
Resolution2.05 Å
3D
structure
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Enzymatic activity
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 A D10 D15 T137 D261 D13 D18 T140 D264
BS02 UA2 A N12 D14 D40 F79 W83 M164 E184 N186 R252 Y257 W260 D261 N15 D17 D43 F82 W86 M167 E187 N189 R255 Y260 W263 D264 MOAD: Ki=0.9nM
PDBbind-CN: -logKd/Ki=9.05,Ki=0.9nM
Gene Ontology
Molecular Function
GO:0008477 purine nucleosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0016799 hydrolase activity, hydrolyzing N-glycosyl compounds
GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
GO:0046872 metal ion binding
Biological Process
GO:0006139 nucleobase-containing compound metabolic process
GO:0006152 purine nucleoside catabolic process
GO:0006166 purine ribonucleoside salvage
Cellular Component
GO:0005829 cytosol
GO:0020015 glycosome

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External links
PDB RCSB:4i72, PDBe:4i72, PDBj:4i72
PDBsum4i72
PubMed23897478
UniProtQ57ZL6

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