2P27

Crystal Structure of Human Pyridoxal Phosphate Phosphatase with Mg2+ at 1.9 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004721	molecular_function	phosphoprotein phosphatase activity
A	0004722	molecular_function	protein serine/threonine phosphatase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005886	cellular_component	plasma membrane
A	0005911	cellular_component	cell-cell junction
A	0006338	biological_process	chromatin remodeling
A	0006357	biological_process	regulation of transcription by RNA polymerase II
A	0006470	biological_process	protein dephosphorylation
A	0007088	biological_process	regulation of mitotic nuclear division
A	0015629	cellular_component	actin cytoskeleton
A	0016311	biological_process	dephosphorylation
A	0016787	molecular_function	hydrolase activity
A	0016791	molecular_function	phosphatase activity
A	0017018	molecular_function	myosin phosphatase activity
A	0030027	cellular_component	lamellipodium
A	0030496	cellular_component	midbody
A	0030836	biological_process	positive regulation of actin filament depolymerization
A	0031072	molecular_function	heat shock protein binding
A	0031247	biological_process	actin rod assembly
A	0031258	cellular_component	lamellipodium membrane
A	0032154	cellular_component	cleavage furrow
A	0032361	biological_process	pyridoxal phosphate catabolic process
A	0032465	biological_process	regulation of cytokinesis
A	0032587	cellular_component	ruffle membrane
A	0033192	molecular_function	calmodulin-dependent protein phosphatase activity
A	0033883	molecular_function	pyridoxal phosphatase activity
A	0042803	molecular_function	protein homodimerization activity
A	0042995	cellular_component	cell projection
A	0046872	molecular_function	metal ion binding
A	0070938	cellular_component	contractile ring
A	0071318	biological_process	cellular response to ATP
A	0098794	cellular_component	postsynapse
A	0098978	cellular_component	glutamatergic synapse
A	0099159	biological_process	regulation of modification of postsynaptic structure
A	0140791	molecular_function	histone H2AXS140 phosphatase activity
A	0180004	molecular_function	RNA polymerase II CTD heptapeptide repeat Y1 phosphatase activity
A	0180005	molecular_function	RNA polymerase II CTD heptapeptide repeat T4 phosphatase activity
A	0180006	molecular_function	RNA polymerase II CTD heptapeptide repeat S2 phosphatase activity
A	0180007	molecular_function	RNA polymerase II CTD heptapeptide repeat S5 phosphatase activity
A	0180008	molecular_function	RNA polymerase II CTD heptapeptide repeat S7 phosphatase activity
A	1990439	molecular_function	MAP kinase serine/threonine phosphatase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 307

Chain	Residue
A	ASP27
A	ASP29
A	ASP240
A	HOH308
A	HOH309
A	HOH310

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:15580268, ECO:0000269|PubMed:18058037, ECO:0007744|PDB:2P27

Chain	Residue	Details
A	ASP27

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:15580268, ECO:0000305|PubMed:18058037, ECO:0007744|PDB:2P27

Chain	Residue	Details
A	ASP29

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site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:18058037, ECO:0007744|PDB:2P27

Chain	Residue	Details
A	ASP27
A	ASP29
A	SER60
A	HIS184
A	LYS215
A	ASP240

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1qh9

Chain	Residue	Details
A	SER136
A	ASP245
A	ARG51
A	ASP27

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