Structure of PDB 3b9g Chain A

Receptor sequence
>3b9gA (length=317) Species: 5699 (Trypanosoma vivax) [Search protein sequence]
SAKNVVLDHDGNLDDFVAMVLLASNTEKVRLIGALCTDADCFVENGFNVT
GKIMCLMHNNMNLPLFPIGKSAATAVNPFPKEWRCLAKNMDDMPILNIPE
NVELWDKIKAENEKYEGQQLLADLVMNSEEKVTICVTGPLSNVAWCIDKY
GEKFTSKVEECVIMGGAVDVRGNVFLPSTDGTAEWNIYWDPASAKTVFGC
PGLRRIMFSLDSTNTVPVRSPYVQRFGEQTNFLLSILVGTMWAMGGGYAW
DALTAAYVVDQKVANVDPVPIDVVVDKQPNEGATVRTDAENYPLTFVARN
PEAEFFLDMLLRSARAC
3D structure
PDB3b9g A Flexible Loop as a Functional Element in the Catalytic Mechanism of Nucleoside Hydrolase from Trypanosoma vivax.
ChainA
Resolution1.4 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 W250 D251
Catalytic site (residue number reindexed from 1) D10 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 D10 D15 T137 D251 D10 D15 T137 D251
BS02 IMH A N12 D14 D40 M164 E184 N186 W250 D251 N12 D14 D40 M164 E184 N186 W250 D251 MOAD: Ki=19uM
PDBbind-CN: -logKd/Ki=4.72,Ki=19uM
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:3b9g, PDBe:3b9g, PDBj:3b9g
PDBsum3b9g
PubMed18519562
UniProtQ9GPQ4

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