Structure of PDB 2cfr Chain A Binding Site BS01

Receptor Information
>2cfr Chain A (length=290) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RCERLRGAALRDVLGRAQGVLFDCDGVLWNGERAVPGAPELLERLARAGK
AALFVSNNSRRARPELALRFARLGFGGLRAEQLFSSALCAARLLRQRLPG
PPDAPGAVFVLGGEGLRAELRAAGLRLAGDPSAAPRVRAVLVGYDEHFSF
AKLREACAHLRDPECLLVATDRDPWHPLSDGSRTPGTGSLAAAVETASGR
QALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRCGMTTVL
TLTGVSRLEEAQAYLAAGQHDLVPHYYVESIADLTEGLED
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 chain2cfr Chain A Residue 1297 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2cfr Crystal Structure of Human Pyridoxal 5'-Phosphate Phosphatase
Resolution2.4 Å
Binding residue
(original residue number in PDB)		D25 D27 D238
Binding residue
(residue number reindexed from 1)		D23 D25 D232
Annotation score1
Enzymatic activity
Enzyme Commision number 3.1.3.16: protein-serine/threonine phosphatase.
3.1.3.74: pyridoxal phosphatase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004721 phosphoprotein phosphatase activity
GO:0004722 protein serine/threonine phosphatase activity
GO:0005515 protein binding
GO:0016787 hydrolase activity
GO:0016791 phosphatase activity
GO:0017018 myosin phosphatase activity
GO:0031072 heat shock protein binding
GO:0033883 pyridoxal phosphatase activity
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
Biological Process
GO:0006470 protein dephosphorylation
GO:0007088 regulation of mitotic nuclear division
GO:0016311 dephosphorylation
GO:0030836 positive regulation of actin filament depolymerization
GO:0031247 actin rod assembly
GO:0032361 pyridoxal phosphate catabolic process
GO:0032465 regulation of cytokinesis
GO:0071318 cellular response to ATP
GO:0099159 regulation of modification of postsynaptic structure
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005856 cytoskeleton
GO:0005886 plasma membrane
GO:0005911 cell-cell junction
GO:0015629 actin cytoskeleton
GO:0030027 lamellipodium
GO:0030496 midbody
GO:0031258 lamellipodium membrane
GO:0032154 cleavage furrow
GO:0032587 ruffle membrane
GO:0042995 cell projection
GO:0070938 contractile ring
GO:0098794 postsynapse
GO:0098978 glutamatergic synapse

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2cfr, PDBe:2cfr, PDBj:2cfr
PDBsum2cfr
PubMed
UniProtQ96GD0|PLPP_HUMAN Chronophin (Gene Name=PDXP)

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