Structure of PDB 4elg Chain B Binding Site BS01

Receptor Information
>4elg Chain B (length=166) Species: 260799 (Bacillus anthracis str. Sterne) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MIVSFMVAMDENRVIGKDNNLPWRLPSELQYVKKTTMGHPLIMGRKNYEA
IGRPLPGRRNIIVTRNEGYHVEGCEVAHSVEEVFELCKNEEEIFIFGGAQ
IYDLFLPYVDKLYITKIHHAFEGDTFFPEMDMTNWKEVFVEKGLTDEKNP
YTYYYHVYEKQQLVPR
Ligand information
Ligand ID52J
InChIInChI=1S/C28H32N6O3/c1-17(2)11-23-22-8-6-5-7-20(22)16-32-34(23)25(35)10-9-19-12-18(14-24(36-3)26(19)37-4)13-21-15-31-28(30)33-27(21)29/h5-10,12,14-17,23H,11,13H2,1-4H3,(H4,29,30,31,33)/b10-9+/t23-/m0/s1
InChIKeyZISYTWICFLBNJQ-ZUTVHTERSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6CC(C)CC1c2ccccc2C=NN1C(=O)C=Cc3cc(cc(c3OC)OC)Cc4cnc(nc4N)N
CACTVS 3.370COc1cc(Cc2cnc(N)nc2N)cc(/C=C/C(=O)N3N=Cc4ccccc4[C@@H]3CC(C)C)c1OC
ACDLabs 12.01O=C(\C=C\c1cc(cc(OC)c1OC)Cc2cnc(nc2N)N)N4N=Cc3ccccc3C4CC(C)C
OpenEye OEToolkits 1.7.6CC(C)C[C@H]1c2ccccc2C=NN1C(=O)/C=C/c3cc(cc(c3OC)OC)Cc4cnc(nc4N)N
CACTVS 3.370COc1cc(Cc2cnc(N)nc2N)cc(C=CC(=O)N3N=Cc4ccccc4[CH]3CC(C)C)c1OC
FormulaC28 H32 N6 O3
Name(2E)-3-{5-[(2,4-diaminopyrimidin-5-yl)methyl]-2,3-dimethoxyphenyl}-1-[(1S)-1-(2-methylpropyl)phthalazin-2(1H)-yl]prop-2-en-1-one;
(S,E)-3-(5-((2,4-diaminopyrimidin-5-yl)methyl)-2,3-dimethoxyphenyl)-1-(1-isobutylphthalazin-2(1H)-yl)prop-2-en-1-one
ChEMBL
DrugBank
ZINCZINC000084668990
PDB chain4elg Chain B Residue 201 [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]
PDB4elg Structure-activity relationship for enantiomers of potent inhibitors of B. anthracis dihydrofolate reductase.
Resolution2.101 Å
Binding residue
(original residue number in PDB)		M6 V7 A8 N20 L21 E28 V32 K33 I51 L55 P56 R58 F96
Binding residue
(residue number reindexed from 1)		M6 V7 A8 N20 L21 E28 V32 K33 I51 L55 P56 R58 F96
Annotation score1
Binding affinityMOAD: Ki=6.9nM
Enzymatic activity
Catalytic site (original residue number in PDB) M6 L21 W23 E28 L29 V32 L55 I93 T115
Catalytic site (residue number reindexed from 1) M6 L21 W23 E28 L29 V32 L55 I93 T115
Enzyme Commision number 1.5.1.3: dihydrofolate reductase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004146 dihydrofolate reductase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0050661 NADP binding
Biological Process
GO:0006730 one-carbon metabolic process
GO:0046452 dihydrofolate metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046655 folic acid metabolic process
Cellular Component
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4elg, PDBe:4elg, PDBj:4elg
PDBsum4elg
PubMed22999981
UniProtQ81R22

[Back to BioLiP]