Structure of PDB 1kie Chain A

Receptor sequence
>1kieA (length=315) Species: 5699 (Trypanosoma vivax) [Search protein sequence]
SAKNVVLDHAGNLDDFVAMVLLASNTEKVRLIGALCTDADCFVENGFNVT
GKIMCLMHNNMNLPLFPIGKSAATAVNPFPKEWRCLAKNMDDMPILNIPE
NVELWDKIKAENEKYEGQQLLADLVMNSEEKVTICVTGPLSNVAWCIDKY
GEKFTSKVEECVIMGGAVDVRGNVFLPSTDGTAEWNIYWDPASAKTVFGC
PGLRRIMFSLDSTNTVPVRSPYVQRFGEQTNFLLSILVGTMWAMCYAWDA
LTAAYVVDQKVANVDPVPIDVVVDKQPNEGATVRTDAENYPLTFVARNPE
AEFFLDMLLRSARAC
3D structure
PDB1kie Enzyme-substrate interactions in the purine-specific nucleoside hydrolase from Trypanosoma vivax.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A10 D15 D40 W83 T137 W185 N186 W260 D261
Catalytic site (residue number reindexed from 1) A10 D15 D40 W83 T137 W185 N186 W248 D249
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 D15 T137 D261 D15 T137 D249
BS02 AD3 A D40 M164 N173 E184 N186 W260 D261 D40 M164 N173 E184 N186 W248 D249
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:1kie, PDBe:1kie, PDBj:1kie
PDBsum1kie
PubMed11854281
UniProtQ9GPQ4

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