Structure of PDB 2pk0 Chain D Binding Site BS01

Receptor Information
>2pk0 Chain D (length=243) Species: 205921 (Streptococcus agalactiae A909) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
YMEISLLTDIGQRRSNNQDFINQFENKAGVPLIILADGMGGHRAGNIASE
MTVTDLGSDWAETDFSELSEIRDWMLVSIETENRKIYELGQSDDYKGMGT
TIEAVAIVGDNIIFAHVGDSRIGIVRQGEYHLLTSDHSLVNELVKAGQLT
EEEAASHPQKNIITQSIGQANPVEPDLGVHLLEEGDYLVVNSDGLTNMLS
NADIATVLTQEKTLDDKNQDLITLANHRGGLDNITVALVYVES
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 chain2pk0 Chain D Residue 506 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2pk0 Structure of Streptococcus agalactiae serine/threonine phosphatase. The subdomain conformation is coupled to the binding of a third metal ion
Resolution2.65 Å
Binding residue
(original residue number in PDB)		D36 G37
Binding residue
(residue number reindexed from 1)		D37 G38
Annotation score1
Enzymatic activity
Enzyme Commision number 3.1.3.16: protein-serine/threonine phosphatase.
Gene Ontology
Molecular Function
GO:0004722 protein serine/threonine phosphatase activity
GO:0016787 hydrolase activity
GO:0016791 phosphatase activity
GO:0017018 myosin phosphatase activity
GO:0046872 metal ion binding
Biological Process
GO:0006470 protein dephosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:2pk0, PDBe:2pk0, PDBj:2pk0
PDBsum2pk0
PubMed17521332
UniProtQ8VQA1

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