Structure of PDB 1lvu Chain B Binding Site BS02

Receptor Information
>1lvu Chain B (length=277) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QNGYTYEDYQDTAKWLLSHTEQRPQVAVICGSGLGGLVNKLTQAQTFDYS
EIPNFPESTVPGHAGRLVFGILNGRACVMMQGRFHMYEGYPFWKVTFPVR
VFRLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFSGQNPLRGPN
EERFGVRFPAMSDAYDRDMRQKAHSTWKQMGEQRELQEGTYVMLGGPNFE
TVAECRLLRNLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYEH
EEVLEAGKQAAQKLEQFVSLLMASIPV
Ligand information
Ligand ID9PP
InChIInChI=1S/C9H15N6O4P/c1-5(19-4-20(16,17)18)2-15-3-12-6-7(10)13-9(11)14-8(6)15/h3,5H,2,4H2,1H3,(H2,16,17,18)(H4,10,11,13,14)/p-2/t5-/m0/s1
InChIKeyLWEKFDHXJHJYGB-YFKPBYRVSA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C[C@@H](Cn1cnc2c1nc(nc2N)N)OCP(=O)([O-])[O-]
ACDLabs 10.04[O-]P([O-])(=O)COC(C)Cn1c2nc(nc(c2nc1)N)N
OpenEye OEToolkits 1.5.0CC(Cn1cnc2c1nc(nc2N)N)OCP(=O)([O-])[O-]
CACTVS 3.341C[CH](Cn1cnc2c(N)nc(N)nc12)OC[P]([O-])([O-])=O
CACTVS 3.341C[C@@H](Cn1cnc2c(N)nc(N)nc12)OC[P]([O-])([O-])=O
FormulaC9 H13 N6 O4 P
Name2,6-DIAMINO-(S)-9-[2-(PHOSPHONOMETHOXY)PROPYL]PURINE
ChEMBL
DrugBankDB02222
ZINC
PDB chain1lvu Chain B Residue 6200 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1lvu Crystal structure of calf spleen purine nucleoside phosphorylase with two full trimers in the asymmetric unit: important implications for the mechanism of catalysis
Resolution2.05 Å
Binding residue
(original residue number in PDB)		G1032 S1033 R1084 H1086 N1115 A1116 A1117 G1118 F1200 E1201 V1217 M1219 S1220 N1243
Binding residue
(residue number reindexed from 1)		G31 S32 R83 H85 N114 A115 A116 G117 F199 E200 V216 M218 S219 N242
Annotation score1
Binding affinityMOAD: Kd=4.8uM
PDBbind-CN: -logKd/Ki=5.32,Kd=4.8uM
Enzymatic activity
Catalytic site (original residue number in PDB) S1033 H1064 Y1088 A1116 M1219 S1220 H1257
Catalytic site (residue number reindexed from 1) S32 H63 Y87 A115 M218 S219 H250
Enzyme Commision number 2.4.2.1: purine-nucleoside phosphorylase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004731 purine-nucleoside phosphorylase activity
GO:0016757 glycosyltransferase activity
GO:0016763 pentosyltransferase activity
GO:0047975 guanosine phosphorylase activity
Biological Process
GO:0006139 nucleobase-containing compound metabolic process
GO:0006166 purine ribonucleoside salvage
GO:0009116 nucleoside metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1lvu, PDBe:1lvu, PDBj:1lvu
PDBsum1lvu
PubMed15342253
UniProtP55859|PNPH_BOVIN Purine nucleoside phosphorylase (Gene Name=PNP)

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