Structure of PDB 2cft Chain A Binding Site BS01

Receptor Information
>2cft Chain A (length=292) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MARCERLRGAALRDVLGRAQGVLFDCDGVLWNGERAVPGAPELLERLARA
GKAALFVSNNSRRARPELALRFARLGFGGLRAEQLFSSALCAARLLRQRL
PGPPDGAVFVLGGEGLRAELRAAGLRLAGDPSAGDGAAPRVRAVLVGYDE
HFSFAKLREACAHLRDPECLLVATDRDPWHPLSDGSRTPGTGSLAAAVET
ASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRCGM
TTVLTLTGVSRLEEAQAYLAAGQHDLVPHYYVESIADLTEGL
Ligand information
Ligand IDPLP
InChIInChI=1S/C8H10NO6P/c1-5-8(11)7(3-10)6(2-9-5)4-15-16(12,13)14/h2-3,11H,4H2,1H3,(H2,12,13,14)
InChIKeyNGVDGCNFYWLIFO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(C=O)c1O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)C=O)O
ACDLabs 10.04O=P(O)(O)OCc1cnc(c(O)c1C=O)C
FormulaC8 H10 N O6 P
NamePYRIDOXAL-5'-PHOSPHATE;
VITAMIN B6 Phosphate
ChEMBLCHEMBL82202
DrugBankDB00114
ZINCZINC000001532514
PDB chain2cft Chain A Residue 1296 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2cft Crystal Structure of Human Pyridoxal 5-Phosphate Phosphatase
Resolution1.8 Å
Binding residue
(original residue number in PDB)		D25 D27 S58 N59 N60 Y150 H182 K213 L294
Binding residue
(residue number reindexed from 1)		D25 D27 S58 N59 N60 Y148 H180 K211 L292
Annotation score3
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:2cft, PDBe:2cft, PDBj:2cft
PDBsum2cft
PubMed
UniProtQ96GD0|PLPP_HUMAN Chronophin (Gene Name=PDXP)

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