Structure of PDB 1kic Chain A

Receptor sequence
>1kicA (length=317) Species: 5699 (Trypanosoma vivax) [Search protein sequence]
SAKNVVLDHAGNLDDFVAMVLLASNTEKVRLIGALCTDADCFVENGFNVT
GKIMCLMHNNMNLPLFPIGKSAATAVNPFPKEWRCLAKNMDDMPILNIPE
NVELWDKIKAENEKYEGQQLLADLVMNSEEKVTICVTGPLSNVAWCIDKY
GEKFTSKVEECVIMGGAVDVRGNVFLPSTDGTAEWNIYWDPASAKTVFGC
PGLRRIMFSLDSTNTVPVRSPYVQRFGEQTNFLLSILVGTMWAMCTYYAW
DALTAAYVVDQKVANVDPVPIDVVVDKQPNEGATVRTDAENYPLTFVARN
PEAEFFLDMLLRSARAC
3D structure
PDB1kic Enzyme-substrate interactions in the purine-specific nucleoside hydrolase from Trypanosoma vivax.
ChainA
Resolution1.6 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 W250 D251
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 D251
BS02 NOS A D40 M164 E184 Y257 W260 D261 D40 M164 E184 Y247 W250 D251
BS03 NOS A R171 F175 L176 D180 G181 R171 F175 L176 D180 G181
BS04 NOS A E44 K109 E113 E44 K109 E113
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:1kic, PDBe:1kic, PDBj:1kic
PDBsum1kic
PubMed11854281
UniProtQ9GPQ4

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