Structure of PDB 4efc Chain A Binding Site BS02

Receptor Information
>4efc Chain A (length=452) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VDYSVDNPLFALSPLDGRYKRQTKALRAFFSEYGFFRYRVLVEVEYFTAL
CKDVPTIVPLRSVTDEQLQKLRKITLDCFSVSSAEEIKRLERVTNHDIKA
VEYFIKERMDTCGLSHVTEFVHFGLTSQDINNTAIPMMIRDAIVTLYLPA
LDGIIGSLTSKLVDWDVPMLARTHGQPASPTNLAKEFVVWIERLREQRRQ
LCEVPTTGKFGGATGNFNAHLVAYPSVNWRAFADMFLAKYLGLKRQQATT
QIENYDHLAALCDACARLHVILIDMCRDVWQYISMGFFKQKVKEGEVGSS
TMPHKVNPIDFENAEGNLALSNALLNFFASKLPISRLQRDLTDSTVLRNL
GVPIGHACVAFASISQGLEKLMISRETISRELSSNWAVVAEGIQTVLRRE
CYPKPYETLKKLTVTEEQVRNFINGLTDISDDVRAELLAITPFTYVGYVP
RF
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain4efc Chain A Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4efc Crystal Structure of Adenylosuccinate Lyase from Trypanosoma Brucei, Tb427tmp.160.5560
Resolution2.0 Å
Binding residue
(original residue number in PDB)		D285 D289
Binding residue
(residue number reindexed from 1)		D274 D278
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H107 T184 H185 S311 K316 E323
Catalytic site (residue number reindexed from 1) H96 T173 H174 S300 K305 E312
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:0046872 metal ion binding
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
Cellular Component
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0020015 glycosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4efc, PDBe:4efc, PDBj:4efc
PDBsum4efc
PubMed
UniProtQ38EJ2

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