Structure of PDB 1yon Chain A Binding Site BS01

Receptor Information
>1yon Chain A (length=292) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKITVLGCGALGQLWLTALCKQGHEVQGWLRVPQPYCSVNLVETDGSIFN
ESLTANDPDFLATSDLLLVTLKAWQVSDAVKSLASTLPVTTPILLIHNGM
GTIEELQNIQQPLLMGTTTHAARRDGNVIIHVANGITHIGPARQQDGDYS
YLADILQTVLPDVAWHNNIRAELWRKLAVNCVINPLTAIWNCPNGELRHH
PQEIMQICEEVAAVIEREGHHTSAEDLRDYVMQVIDATAENISSMLQDIR
ALRHTEIDYINGFLLRRARAHGIAVPENTRLFEMVKRKESEY
Ligand information
Ligand IDA2R
InChIInChI=1S/C15H24N5O17P3/c16-12-7-13(18-3-17-12)20(4-19-7)14-11(36-38(25,26)27)9(22)6(34-14)2-33-40(30,31)37-39(28,29)32-1-5-8(21)10(23)15(24)35-5/h3-6,8-11,14-15,21-24H,1-2H2,(H,28,29)(H,30,31)(H2,16,17,18)(H2,25,26,27)/t5-,6-,8-,9-,10-,11-,14-,15-/m1/s1
InChIKeyICNHOLCERMYLRZ-KEOHHSTQSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)OC[CH]4O[CH](O)[CH](O)[CH]4O)[CH](O)[CH]3O[P](O)(O)=O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]4[C@H]([C@H]([C@@H](O4)O)O)O)O)OP(=O)(O)O)N
ACDLabs 10.04O=P(O)(O)OC3C(O)C(OC3n1c2ncnc(N)c2nc1)COP(=O)(O)OP(=O)(O)OCC4OC(O)C(O)C4O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)O)O)O)O)OP(=O)(O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P@](O)(=O)OC[C@H]4O[C@@H](O)[C@H](O)[C@@H]4O)[C@@H](O)[C@H]3O[P](O)(O)=O
FormulaC15 H24 N5 O17 P3
Name[(2R,3R,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3-HYDROXY-4-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]METHYL [(2R,3S,4R,5R)-3,4,5-TRIHYDROXYTETRAHYDROFURAN-2-YL]METHYL DIHYDROGEN DIPHOSPHATE
ChEMBL
DrugBank
ZINCZINC000044460250
PDB chain1yon Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1yon pH-tuneable binding of 2'-phospho-ADP-ribose to ketopantoate reductase: a structural and calorimetric study.
Resolution1.95 Å
Binding residue
(original residue number in PDB)		G9 A10 L11 L71 K72 H97 N98 T118 S244 R253 E256
Binding residue
(residue number reindexed from 1)		G9 A10 L11 L71 K72 H97 N98 T118 S244 R253 E256
Annotation score3
Binding affinityMOAD: Kd=61uM
PDBbind-CN: -logKd/Ki=4.21,Kd=61uM
Enzymatic activity
Catalytic site (original residue number in PDB) K176
Catalytic site (residue number reindexed from 1) K176
Enzyme Commision number 1.1.1.169: 2-dehydropantoate 2-reductase.
Gene Ontology
Molecular Function
GO:0008677 2-dehydropantoate 2-reductase activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0050661 NADP binding
Biological Process
GO:0015940 pantothenate biosynthetic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1yon, PDBe:1yon, PDBj:1yon
PDBsum1yon
PubMed17242510
UniProtP0A9J4|PANE_ECOLI 2-dehydropantoate 2-reductase (Gene Name=panE)

[Back to BioLiP]