Structure of PDB 5nxa Chain B Binding Site BS02

Receptor Information
>5nxa Chain B (length=415) Species: 63221 (Homo sapiens neanderthalensis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GSPDSYRSPLASRYASPEMCFVFSDRYKFRTWRQLWLWLGATSCYVGDNT
DLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVG
KRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKV
EQLDKMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLASLGASVHKICTDI
RLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPL
QTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVI
ERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKQEGG
DNDLIERIQADAYFSPIHSQLDHLLDPSSFTGRASQQVQRFLEEEVYPLL
KPYESVMKVKAELCL
Ligand information
Ligand IDSSS
InChIInChI=1S/C13H19N4O12P/c14-10-7(11(22)16-4(13(23)24)1-6(18)19)15-3-17(10)12-9(21)8(20)5(29-12)2-28-30(25,26)27/h3-5,8-9,12,20-21H,1-2,14H2,(H,16,22)(H,18,19)(H,23,24)(H2,25,26,27)/t4-,5+,8+,9-,12+/m0/s1
InChIKeyNAQGHJTUZRHGAC-PSYSQGJASA-N
SMILES
SoftwareSMILES
CACTVS 3.341Nc1n(cnc1C(=O)N[CH](CC(O)=O)C(O)=O)[CH]2O[CH](CO[P](O)(O)=O)[CH](O)[CH]2O
CACTVS 3.341Nc1n(cnc1C(=O)N[C@@H](CC(O)=O)C(O)=O)[C@@H]2O[C@H](CO[P](O)(O)=O)[C@@H](O)[C@@H]2O
OpenEye OEToolkits 1.5.0c1nc(c(n1[C@H]2[C@H]([C@@H]([C@H](O2)COP(=O)(O)O)O)O)N)C(=O)N[C@@H](CC(=O)O)C(=O)O
ACDLabs 10.04O=C(O)CC(C(=O)O)NC(=O)c1ncn(c1N)C2OC(C(O)C2O)COP(=O)(O)O
OpenEye OEToolkits 1.5.0c1nc(c(n1C2C(C(C(O2)COP(=O)(O)O)O)O)N)C(=O)NC(CC(=O)O)C(=O)O
FormulaC13 H19 N4 O12 P
NameN-{[5-AMINO-1-(5-O-PHOSPHONO-BETA-D-ARABINOFURANOSYL)-1H-IMIDAZOL-4-YL]CARBONYL}-L-ASPARTIC ACID;
N-{[5-AMINO-1-(5-O-PHOSPHONO-BETA-D-ARABINOFURANOSYL)-1H-IMIDAZOL-4-YL]CARBONYL}-L-ASPARTIC ACID
ChEMBL
DrugBank
ZINCZINC000038191900
PDB chain5nxa Chain B Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5nxa Molecular comparison of Neanderthal and Modern Human adenylosuccinate lyase.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		S112 Q241 L331 S334 A335 R338
Binding residue
(residue number reindexed from 1)		S43 Q172 L262 S265 A266 R269
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) T158 H159 S290 K295 E302
Catalytic site (residue number reindexed from 1) T89 H90 S221 K226 E233
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:0006189 'de novo' IMP biosynthetic process
GO:0009152 purine ribonucleotide biosynthetic process
GO:0009168 purine ribonucleoside monophosphate biosynthetic process
GO:0044208 'de novo' AMP biosynthetic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5nxa, PDBe:5nxa, PDBj:5nxa
PDBsum5nxa
PubMed30573755
UniProtA0A384E0N4

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