Structure of PDB 3qfx Chain B Binding Site BS01

Receptor Information
>3qfx Chain B (length=218) Species: 31286 (Trypanosoma brucei rhodesiense) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PPLRPFSVVVASDEKGGIGDGGTIPWEIPEDMQYFRRVTTNLRGKNVKPS
PSKRNAVVMGRKTWDSLPPKFRPLSNRLNVVLSRSATKEQLLAGIPDPIK
RAEAANDVVAVNGGLEDALRMLVSKEHTSSIETVFCIGGGTIYKQALCAP
CVNVLQAIHRTVVRPASNSCSVFFDIPAAGTKTPEGLELVRESITDERVS
TGAGGKKYQFEKLVPRNS
Ligand information
Ligand IDNDP
InChIInChI=1S/C21H30N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1,3-4,7-8,10-11,13-16,20-21,29-31H,2,5-6H2,(H2,23,32)(H,36,37)(H,38,39)(H2,22,24,25)(H2,33,34,35)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyACFIXJIJDZMPPO-NNYOXOHSSA-N
SMILES
SoftwareSMILES
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)N5C=CCC(=C5)C(=O)N)O)O)O)OP(=O)(O)O)N
CACTVS 3.341NC(=O)C1=CN(C=CC1)[CH]2O[CH](CO[P](O)(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O[P](O)(O)=O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
CACTVS 3.341NC(=O)C1=CN(C=CC1)[C@@H]2O[C@H](CO[P@@](O)(=O)O[P@](O)(=O)OC[C@H]3O[C@H]([C@H](O[P](O)(O)=O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)N5C=CCC(=C5)C(=O)N)O)O)O)OP(=O)(O)O)N
FormulaC21 H30 N7 O17 P3
NameNADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
ChEMBLCHEMBL407009
DrugBankDB02338
ZINCZINC000008215411
PDB chain3qfx Chain B Residue 701 [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]
PDB3qfx Trypanosomal dihydrofolate reductase reveals natural antifolate resistance
Resolution2.2 Å
Binding residue
(original residue number in PDB)		V33 A34 I41 G44 G45 T46 G83 R84 K85 T86 L105 S106 R107 G136 G137 I160 G162 G163 T164 I165 Y166
Binding residue
(residue number reindexed from 1)		V10 A11 I18 G21 G22 T23 G60 R61 K62 T63 L82 S83 R84 G113 G114 I137 G139 G140 T141 I142 Y143
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) I47 D54
Catalytic site (residue number reindexed from 1) I24 D31
Enzyme Commision number 1.5.1.3: dihydrofolate reductase.
2.1.1.45: thymidylate synthase.
Gene Ontology
Molecular Function
GO:0004146 dihydrofolate reductase activity
GO:0050661 NADP binding
Biological Process
GO:0046654 tetrahydrofolate biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3qfx, PDBe:3qfx, PDBj:3qfx
PDBsum3qfx
PubMed21650210
UniProtQ27783|DRTS_TRYBB Bifunctional dihydrofolate reductase-thymidylate synthase

[Back to BioLiP]