Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2BDX

X-ray Crystal Structure of dihydromicrocystin-LA bound to Protein Phosphatase-1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000070	biological_process	mitotic sister chromatid segregation
A	0000165	biological_process	MAPK cascade
A	0000775	cellular_component	chromosome, centromeric region
A	0000776	cellular_component	kinetochore
A	0000781	cellular_component	chromosome, telomeric region
A	0001824	biological_process	blastocyst development
A	0003723	molecular_function	RNA binding
A	0004721	molecular_function	phosphoprotein phosphatase activity
A	0004722	molecular_function	protein serine/threonine phosphatase activity
A	0005515	molecular_function	protein binding
A	0005521	molecular_function	lamin binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005694	cellular_component	chromosome
A	0005730	cellular_component	nucleolus
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005741	cellular_component	mitochondrial outer membrane
A	0005815	cellular_component	microtubule organizing center
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005925	cellular_component	focal adhesion
A	0005977	biological_process	glycogen metabolic process
A	0006338	biological_process	chromatin remodeling
A	0006357	biological_process	regulation of transcription by RNA polymerase II
A	0006470	biological_process	protein dephosphorylation
A	0007283	biological_process	spermatogenesis
A	0008157	molecular_function	protein phosphatase 1 binding
A	0016607	cellular_component	nuclear speck
A	0016787	molecular_function	hydrolase activity
A	0016791	molecular_function	phosphatase activity
A	0017018	molecular_function	myosin phosphatase activity
A	0019901	molecular_function	protein kinase binding
A	0019903	molecular_function	protein phosphatase binding
A	0019904	molecular_function	protein domain specific binding
A	0030182	biological_process	neuron differentiation
A	0030496	cellular_component	midbody
A	0032154	cellular_component	cleavage furrow
A	0032922	biological_process	circadian regulation of gene expression
A	0032991	cellular_component	protein-containing complex
A	0033192	molecular_function	calmodulin-dependent protein phosphatase activity
A	0042752	biological_process	regulation of circadian rhythm
A	0043153	biological_process	entrainment of circadian clock by photoperiod
A	0043197	cellular_component	dendritic spine
A	0044877	molecular_function	protein-containing complex binding
A	0046822	biological_process	regulation of nucleocytoplasmic transport
A	0046872	molecular_function	metal ion binding
A	0048511	biological_process	rhythmic process
A	0051301	biological_process	cell division
A	0060252	biological_process	positive regulation of glial cell proliferation
A	0072357	cellular_component	PTW/PP1 phosphatase complex
A	0098793	cellular_component	presynapse
A	0098794	cellular_component	postsynapse
A	0098978	cellular_component	glutamatergic synapse
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 MN A 400

Chain	Residue
A	ASP92
A	ASN124
A	HIS173
A	HIS248
A	MN401
A	HOH523

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN A 401

Chain	Residue
A	MN400
A	HOH523
A	HOH524
A	ASP64
A	HIS66
A	ASP92

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR CHAIN B OF DIHYDROMICROCYSTIN-LA

Chain	Residue
A	SER129
A	TYR134
A	GLN181
A	SER182
A	GLU184
A	GLN185
A	ARG188
A	ASP220
A	ARG221
A	VAL223
A	TYR272
A	GLU275
A	PHE276
A	HOH514
A	HOH524

Functional Information from PROSITE/UniProt

site_id	PS00125
Number of Residues	6
Details	SER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE

Chain	Residue	Details
A	LEU121-GLU126

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000269\|PubMed:7500362

Chain	Residue	Details
A	HIS125

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:11535607, ECO:0000269\|PubMed:15280359

Chain	Residue	Details
A	ASP64
A	HIS66
A	ASP92
A	ASN124
A	HIS173
A	HIS248

site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Inhibition by microcystin toxin binding

Chain	Residue	Details
A	CYS273

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N-acetylalanine => ECO:0000269\|Ref.3, ECO:0000269\|Ref.4, ECO:0007744\|PubMed:22814378, ECO:0007744\|PubMed:25944712

Chain	Residue	Details
A	ALA2

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:18669648

Chain	Residue	Details
A	THR307

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:23186163, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	THR311

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1aui

Chain	Residue	Details
A	ASP95
A	HIS125

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