Structure of PDB 2j82 Chain A

Receptor sequence
>2j82A (length=221) Species: 32046 (Synechococcus elongatus) [Search protein sequence]
MDVAGLTDCGLIRKSNQDAFYIDEKHQRFFIVADGMAGGEEASRLAVDHI
RQYLETHLEDLQHDPVTLLRQAFLAANHAIVEQQRQNSARADMGTTAVVI
LLDEKGDRAWCAHVGDSRIYRWRKDQLQQITSDHTWIAQARHVLSQCLGR
EDLSQIDIQPIDLEPGDRLLLCSDGLTEELTDDVISIYLSEPNVQKAAAA
LVDAAKTHGGRDNVTVVVISV
3D structure
PDB2j82 Structural Analysis of the Pp2C Phosphatase Tppha from Thermosynechococcus Elongatus: A Flexible Flap Subdomain Controls Access to the Catalytic Site.
ChainA
Resolution1.28 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 CA A D1034 G1035 D34 G35
BS02 MG A D1034 D1193 D1231 D34 D174 D212
BS03 CA A D1034 D1193 D1231 D34 D174 D212
BS04 MG A D1119 D1193 D116 D174
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:2j82, PDBe:2j82, PDBj:2j82
PDBsum2j82
PubMed18164312
UniProtQ8DGS1

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