Structure of PDB 4mx2 Chain B Binding Site BS01

Receptor Information
>4mx2 Chain B (length=439) Species: 5661 (Leishmania donovani) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EISQDSPLYSLSPLDGRYKRDTTPLRAYFSEYALFKYRVQVEVLYFEALC
KEVPAITQLRGVTDAQLGELRATTFENFAVDDAKIIKGIEAVTNHDIKAV
EYYLKDKMSACGLEAEKEFIHFGLTSQDINNTSIPMLLRDALHHHYIPTL
DQLIALLKSKLPEWDVPMLARTHGQPASPTNLAKEFMVWIERLEEQRTML
LSIPNTGKFGGATGNFNAHLCAYPGVNWLDFGELFLSKYLGLRRQRYTTQ
IEHYDNLAAICDACARLHTILMDLAKDVWQYISLGYFDQKVREVGVNPID
FENAEGNLGMSNAVLGFLSAKLPISRLQRDLTDSTVLRNLGVPLSHALIA
FASLRRGIDKLLLNKDVIASDLEGNWAVVAEGIQTVLRREGYPKPYEALK
DHVTEETVHRFVQQLITEEVRQELLAITPFTYVGYTAHP
Ligand information
Ligand IDAMP
InChIInChI=1S/C10H14N5O7P/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(22-10)1-21-23(18,19)20/h2-4,6-7,10,16-17H,1H2,(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyUDMBCSSLTHHNCD-KQYNXXCUSA-N
SMILES
SoftwareSMILES
CACTVS 3.370Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(O)=O)[CH](O)[CH]3O
CACTVS 3.370Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.7.6c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O)O)O)O)N
ACDLabs 12.01O=P(O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.7.6c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)O)O)O)N
FormulaC10 H14 N5 O7 P
NameADENOSINE MONOPHOSPHATE
ChEMBLCHEMBL752
DrugBankDB00131
ZINCZINC000003860156
PDB chain4mx2 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

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PDB4mx2 Crystal Structure of adenylosuccinate lyase from Leishmania donovani
Resolution1.9 Å
Binding residue
(original residue number in PDB)		R40 Y41 I331 N335
Binding residue
(residue number reindexed from 1)		R17 Y18 I299 N303
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) H118 T195 H196 E334
Catalytic site (residue number reindexed from 1) H95 T172 H173 E302
Enzyme Commision number 4.3.2.2: adenylosuccinate lyase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0004018 N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
GO:0016829 lyase activity
GO:0070626 (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006188 IMP biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process
GO:0009152 purine ribonucleotide biosynthetic process
GO:0044208 'de novo' AMP biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4mx2, PDBe:4mx2, PDBj:4mx2
PDBsum4mx2
PubMed
UniProtA7LBL3

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