Structure of PDB 1ktg Chain B Binding Site BS02

Receptor Information
>1ktg Chain B (length=132) Species: 6239 (Caenorhabditis elegans) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KAAGLVIYRKLAGKIEFLLLQASYPPHHWTPPKGHVDPGEDEWQAAIRET
KEEANITKEQLTIHEDCHETLFYEAPKSVKYWLAKLNNPDDVQLSHEHQN
WKWCELEDAIKIADYAEMGSLLRKFSAFLAGF
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 chain1ktg Chain B Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1ktg The crystal structure of diadenosine tetraphosphate hydrolase from Caenorhabditis elegans in free and binary complex forms
Resolution1.8 Å
Binding residue
(original residue number in PDB)		K36 E56
Binding residue
(residue number reindexed from 1)		K33 E53
Annotation score1
Enzymatic activity
Enzyme Commision number 3.6.1.-
Gene Ontology
Molecular Function
GO:0004081 bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity
GO:0005524 ATP binding
GO:0008796 bis(5'-nucleosyl)-tetraphosphatase activity
GO:0016787 hydrolase activity
GO:0043135 5-phosphoribosyl 1-pyrophosphate pyrophosphatase activity
Biological Process
GO:0006167 AMP biosynthetic process
GO:0006172 ADP biosynthetic process
GO:0006754 ATP biosynthetic process
GO:0006915 apoptotic process
GO:0015967 diadenosine tetraphosphate catabolic process
GO:0019693 ribose phosphate metabolic process
Cellular Component
GO:0005575 cellular_component

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ktg, PDBe:1ktg, PDBj:1ktg
PDBsum1ktg
PubMed11937063
UniProtQ9U2M7|AP4A_CAEEL Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical] (Gene Name=ndx-4)

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