BioLiP

Structure of PDB 4i74 Chain A

Receptor sequence

>4i74A (length=327) [Search protein sequence]

GSHMAKTVILDHDGNKDDFVAMILLLSNPKKVNLIGCICTDADCFVENGF
DVTGKIMCAMHRLIKTPLFPIGKSTATAVNAFPTEWRFSAKNLDDMPFLN
IVEDVALWEKLKPENEAHNGQQLLADLVMKSKEKVTVCVTGPLSNMAWCI
EKYGEAFTSKVEECVIMGGAVDVGGNVFLPTTDGSAEWNIYWDPPAAKKV
LCCPNIRCVLFSLDATNTVPVRSVDVKGFGAQNQYLLSQMVGTMWAMSTH
EEILRDGDAYYAWDALTAAYILEPTIATLEPVALDVDVSKGKSEGRTPRA
SGPCVHVARNPSKQMFHDLVFASTRVC

3D structure

PDB

4i74 Structures of purine nucleosidase from Trypanosoma brucei bound to isozyme-specific trypanocidals and a novel metalorganic inhibitor

Chain

Resolution

1.68 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	MBY	A	N12 D14 D40 F79 W83 M164 N173 E184 W185 N186 E248 E249 W260 D261	N15 D17 D43 F82 W86 M167 N176 E187 W188 N189 E251 E252 W263 D264	PDBbind-CN: -logKd/Ki=6.72,Ki=190nM

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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Molecular Function

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Biological Process

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Cellular Component

PDB	RCSB:4i74, PDBe:4i74, PDBj:4i74
PDBsum	4i74
PubMed	23897478
UniProt	Q57ZL6