Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4BX3

Crystal Structure of murine Chronophin (Pyridoxal Phosphate Phosphatase)

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	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	0019838	molecular_function	growth factor binding
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	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
B	0000287	molecular_function	magnesium ion binding
B	0004721	molecular_function	phosphoprotein phosphatase activity
B	0004722	molecular_function	protein serine/threonine phosphatase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005856	cellular_component	cytoskeleton
B	0005886	cellular_component	plasma membrane
B	0005911	cellular_component	cell-cell junction
B	0006470	biological_process	protein dephosphorylation
B	0007088	biological_process	regulation of mitotic nuclear division
B	0015629	cellular_component	actin cytoskeleton
B	0016311	biological_process	dephosphorylation
B	0016787	molecular_function	hydrolase activity
B	0016791	molecular_function	phosphatase activity
B	0017018	molecular_function	myosin phosphatase activity
B	0019838	molecular_function	growth factor binding
B	0030027	cellular_component	lamellipodium
B	0030496	cellular_component	midbody
B	0030836	biological_process	positive regulation of actin filament depolymerization
B	0031072	molecular_function	heat shock protein binding
B	0031247	biological_process	actin rod assembly
B	0031258	cellular_component	lamellipodium membrane
B	0032154	cellular_component	cleavage furrow
B	0032361	biological_process	pyridoxal phosphate catabolic process
B	0032465	biological_process	regulation of cytokinesis
B	0032587	cellular_component	ruffle membrane
B	0033883	molecular_function	pyridoxal phosphatase activity
B	0042803	molecular_function	protein homodimerization activity
B	0042995	cellular_component	cell projection
B	0046872	molecular_function	metal ion binding
B	0070938	cellular_component	contractile ring
B	0071318	biological_process	cellular response to ATP
B	0098794	cellular_component	postsynapse
B	0098978	cellular_component	glutamatergic synapse
B	0099159	biological_process	regulation of modification of postsynaptic structure

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 301

Chain	Residue
A	ASP25
A	ASP27
A	ASP234
A	HOH2010
A	HOH2011
A	HOH2012

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 302

Chain	Residue
B	HOH2004
B	HOH2005
B	HOH2006
B	ASP25
B	ASP27
B	ASP234

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 1292

Chain	Residue
A	ARG62
A	TYR146
A	HIS178

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 1292

Chain	Residue
B	ARG174
B	VAL206
B	HOH2074

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000305\|PubMed:24338687, ECO:0000305\|PubMed:25783190, ECO:0007744\|PDB:4BX2, ECO:0007744\|PDB:5AES

Chain	Residue	Details
A	ASP25
B	ASP25

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000305\|PubMed:24338687, ECO:0000305\|PubMed:25783190, ECO:0007744\|PDB:4BX2, ECO:0007744\|PDB:5AES

Chain	Residue	Details
A	ASP27
B	ASP27

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:24338473, ECO:0000269\|PubMed:24338687, ECO:0000269\|PubMed:25783190, ECO:0007744\|PDB:4BKM, ECO:0007744\|PDB:4BX0, ECO:0007744\|PDB:4BX2, ECO:0007744\|PDB:4BX3, ECO:0007744\|PDB:5AES

Chain	Residue	Details
B	ASP27
B	ASP234
A	ASP25
A	ASP27
A	ASP234
B	ASP25

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:24338687, ECO:0000269\|PubMed:25783190, ECO:0007744\|PDB:4BX2, ECO:0007744\|PDB:5AES

Chain	Residue	Details
B	SER58
B	LYS209
A	SER58
A	LYS209

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:25783190, ECO:0007744\|PDB:5AES

Chain	Residue	Details
A	HIS178
B	HIS178

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)