Structure of PDB 2pk0 Chain D

Receptor sequence
>2pk0D (length=243) Species: 205921 (Streptococcus agalactiae A909) [Search protein sequence]
YMEISLLTDIGQRRSNNQDFINQFENKAGVPLIILADGMGGHRAGNIASE
MTVTDLGSDWAETDFSELSEIRDWMLVSIETENRKIYELGQSDDYKGMGT
TIEAVAIVGDNIIFAHVGDSRIGIVRQGEYHLLTSDHSLVNELVKAGQLT
EEEAASHPQKNIITQSIGQANPVEPDLGVHLLEEGDYLVVNSDGLTNMLS
NADIATVLTQEKTLDDKNQDLITLANHRGGLDNITVALVYVES
3D structure
PDB2pk0 Structure of Streptococcus agalactiae serine/threonine phosphatase. The subdomain conformation is coupled to the binding of a third metal ion
ChainD
Resolution2.65 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.1.3.16: protein-serine/threonine phosphatase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MG D D36 G37 D37 G38
BS02 MG D D36 D192 D231 D37 D193 D232
BS03 MG D D118 D192 D119 D193
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
View graph for
Biological Process
External links
PDB RCSB:2pk0, PDBe:2pk0, PDBj:2pk0
PDBsum2pk0
PubMed17521332
UniProtQ8VQA1

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