Structure of PDB 2ff2 Chain B

Receptor sequence
>2ff2B (length=327) Species: 5699 (Trypanosoma vivax) [Search protein sequence]
SAKNVVLDHDGNLDDFVAMVLLASNTEKVRLIGALCTDADCFVENGFNVT
GKIMCLMHNNMNLPLFPIGKSAATAVNPFPKEWRCLAKNMDDMPILNIPE
NVELWDKIKAENEKYEGQQLLADLVMNSEEKVTICVTGPLSNVAWCIDKY
GEKFTSKVEECVIMGGAVDVRGNVFLPSTDGTAEWNIYWDPASAKTVFGC
PGLRRIMFSLDSTNTVPVRSPYVQRFGEQTNFLLSILVGTMWAMCTHCEL
LRDGDGYYAWDALTAAYVVDQKVANVDPVPIDVVVDKQPNEGATVRTDAE
NYPLTFVARNPEAEFFLDMLLRSARAC
3D structure
PDB2ff2 Transition-state Complex of the Purine-specific Nucleoside Hydrolase of T.vivax: Enzyme Conformational Changes and Implications for Catalysis.
ChainB
Resolution2.2 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 W260 D261
Catalytic site (residue number reindexed from 1) D10 D15 D40 W83 T137 W185 N186 W260 D261
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 B D10 D15 T137 D261 D10 D15 T137 D261
BS02 IMH B N12 D14 D40 W83 M164 N173 E184 N186 R252 Y257 W260 D261 N12 D14 D40 W83 M164 N173 E184 N186 R252 Y257 W260 D261 MOAD: Ki=6.2nM
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
View graph for
Biological Process
External links
PDB RCSB:2ff2, PDBe:2ff2, PDBj:2ff2
PDBsum2ff2
PubMed16630632
UniProtQ9GPQ4

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