Structure of PDB 7whs Chain F Binding Site BS01

Receptor Information
>7whs Chain F (length=366) Species: 5661 (Leishmania donovani) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MRAVILVGGFGTRLRPLTLTTPKPLVPFCNKPMIIHQIEALKAVGVTEVI
LAVAYRPEAMKEQMDEWSRKLGVSFVFSVEEEPLGTAGPLALARDILMQD
DKPFFVLNSDVTCTFPMQELLDFHKAHGGEGTIMVSQVTQWEKYGVVVYS
PQNYQIERFVEKPSRFLGDRINAGIYIFNKSILDRIPPRRASIEKEIFPA
MAAEGQLYAFNLEGFWMDVGQPKDYILGMTKFIPSLVHGNRETEAVEHQR
GGRFTVIGASLIDPSAKIGDGAVIGPYASIGANCVIGESCRIDNAAILEN
SKVGKGTMVSRSIVGWNNRIGSWCHIKDISVLGDDVEVKDGVILIGTKVL
PNKDVGEHRFEPGIIM
Ligand information
Ligand IDGTP
InChIInChI=1S/C10H16N5O14P3/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(27-9)1-26-31(22,23)29-32(24,25)28-30(19,20)21/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H,24,25)(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1
InChIKeyXKMLYUALXHKNFT-UUOKFMHZSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@](=O)(O)OP(=O)(O)O)O)O)N=C(NC2=O)N
CACTVS 3.370NC1=Nc2n(cnc2C(=O)N1)[C@@H]3O[C@H](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
CACTVS 3.370NC1=Nc2n(cnc2C(=O)N1)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
OpenEye OEToolkits 1.7.6c1nc2c(n1C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O)N=C(NC2=O)N
ACDLabs 12.01O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c2N=C(N)NC1=O)C(O)C3O
FormulaC10 H16 N5 O14 P3
NameGUANOSINE-5'-TRIPHOSPHATE
ChEMBLCHEMBL1233147
DrugBankDB04137
ZINCZINC000060094177
PDB chain7whs Chain F Residue 401 [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]
PDB7whs Structural insights into selective inhibition of leishmanial GDP-mannose pyrophosphorylase.
Resolution3.1 Å
Binding residue
(original residue number in PDB)		L14 G16 G17 G19 R21 K31 A60 G93 N116 D118
Binding residue
(residue number reindexed from 1)		L6 G8 G9 G11 R13 K23 A52 G85 N108 D110
Annotation score4
Enzymatic activity
Enzyme Commision number 2.7.7.13: mannose-1-phosphate guanylyltransferase.
Gene Ontology
Molecular Function
GO:0004475 mannose-1-phosphate guanylyltransferase (GTP) activity
GO:0005525 GTP binding
GO:0016740 transferase activity
Biological Process
GO:0006486 protein glycosylation
GO:0009058 biosynthetic process
GO:0009298 GDP-mannose 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:7whs, PDBe:7whs, PDBj:7whs
PDBsum7whs
PubMed36038534
UniProtE9BG32

[Back to BioLiP]