Structure of PDB 2ff2 Chain A Binding Site BS02

Receptor Information
>2ff2 Chain A (length=326) Species: 5699 (Trypanosoma vivax) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AKNVVLDHDGNLDDFVAMVLLASNTEKVRLIGALCTDADCFVENGFNVTG
KIMCLMHNNMNLPLFPIGKSAATAVNPFPKEWRCLAKNMDDMPILNIPEN
VELWDKIKAENEKYEGQQLLADLVMNSEEKVTICVTGPLSNVAWCIDKYG
EKFTSKVEECVIMGGAVDVRGNVFLPSTDGTAEWNIYWDPASAKTVFGCP
GLRRIMFSLDSTNTVPVRSPYVQRFGEQTNFLLSILVGTMWAMCTHCELL
RDGDGYYAWDALTAAYVVDQKVANVDPVPIDVVVDKQPNEGATVRTDAEN
YPLTFVARNPEAEFFLDMLLRSARAC
Ligand information
Ligand IDIMH
InChIInChI=1S/C11H14N4O4/c16-2-5-9(17)10(18)7(15-5)4-1-12-8-6(4)13-3-14-11(8)19/h1,3,5,7,9-10,12,15-18H,2H2,(H,13,14,19)/t5-,7+,9-,10+/m1/s1
InChIKeyIWKXDMQDITUYRK-KUBHLMPHSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.7c1c(c2c([nH]1)C(=O)NC=N2)C3C(C(C(N3)CO)O)O
CACTVS 3.385OC[C@H]1N[C@H]([C@H](O)[C@@H]1O)c2c[nH]c3C(=O)NC=Nc23
ACDLabs 12.01OC1C(NC(CO)C1O)c1c[NH]c2c1N=CNC2=O
OpenEye OEToolkits 2.0.7c1c(c2c([nH]1)C(=O)NC=N2)[C@H]3[C@@H]([C@@H]([C@H](N3)CO)O)O
CACTVS 3.385OC[CH]1N[CH]([CH](O)[CH]1O)c2c[nH]c3C(=O)NC=Nc23
FormulaC11 H14 N4 O4
Name1,4-DIDEOXY-4-AZA-1-(S)-(9-DEAZAHYPOXANTHIN-9-YL)-D-RIBITOL;
Forodesine;
Immucillin H
ChEMBLCHEMBL218291
DrugBankDB06185
ZINCZINC000013492899
PDB chain2ff2 Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2ff2 Transition-state Complex of the Purine-specific Nucleoside Hydrolase of T.vivax: Enzyme Conformational Changes and Implications for Catalysis.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		N12 D14 D40 W83 M164 E184 N186 R252 Y257 W260 D261
Binding residue
(residue number reindexed from 1)		N11 D13 D39 W82 M163 E183 N185 R251 Y256 W259 D260
Annotation score1
Binding affinityMOAD: Ki=6.2nM
PDBbind-CN: -logKd/Ki=8.21,Ki=6.2nM
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) D9 D14 D39 W82 T136 W184 N185 W259 D260
Enzyme Commision number 3.2.2.1: purine nucleosidase.
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2ff2, PDBe:2ff2, PDBj:2ff2
PDBsum2ff2
PubMed16630632
UniProtQ9GPQ4

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