Structure of PDB 2j86 Chain A Binding Site BS02

Receptor Information
>2j86 Chain A (length=235) Species: 32046 (Synechococcus elongatus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MDVAGLTDCGLIRKSNQDAFYIDEKHQRFFIVADGMGGHAGGEEASRLAV
DHIRQYLETHLEDLQHDPVTLLRQAFLAANHAIVEQQRQNSARADMGTTA
VVILLDEKGDRAWCAHVGDSRIYRWRKDQLQQITSDHTWIAQAVQIEQAR
QHPWRHVLSQCLGREDLSQIDIQPIDLEPGDRLLLCSDGLTEELTDDVIS
IYLSEPNVQKAAAALVDAAKTHGGRDNVTVVVISV
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 chain2j86 Chain A Residue 1242 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2j86 Structural Analysis of the Pp2C Phosphatase Tppha from Thermosynechococcus Elongatus: A Flexible Flap Subdomain Controls Access to the Catalytic Site.
Resolution3.05 Å
Binding residue
(original residue number in PDB)		D34 D193 D231
Binding residue
(residue number reindexed from 1)		D34 D188 D226
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:0005515 protein binding
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:2j86, PDBe:2j86, PDBj:2j86
PDBsum2j86
PubMed18164312
UniProtQ8DGS1

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