3FXL

Crystal Structure of Human Protein phosphatase 1A (PPM1A) Bound with Citrate at 1 mM of Mn2+

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
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	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006470	biological_process	protein dephosphorylation
A	0006499	biological_process	N-terminal protein myristoylation
A	0006611	biological_process	protein export from nucleus
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0030145	molecular_function	manganese ion binding
A	0030512	biological_process	negative regulation of transforming growth factor beta receptor signaling pathway
A	0030514	biological_process	negative regulation of BMP signaling pathway
A	0033192	molecular_function	calmodulin-dependent protein phosphatase activity
A	0043122	biological_process	regulation of canonical NF-kappaB signal transduction
A	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
A	0043124	biological_process	negative regulation of canonical NF-kappaB signal transduction
A	0043169	molecular_function	cation binding
A	0045893	biological_process	positive regulation of DNA-templated transcription
A	0046827	biological_process	positive regulation of protein export from nucleus
A	0046872	molecular_function	metal ion binding
A	0051726	biological_process	regulation of cell cycle
A	0070412	molecular_function	R-SMAD binding
A	0071560	biological_process	cellular response to transforming growth factor beta stimulus
A	0090263	biological_process	positive regulation of canonical Wnt signaling pathway
A	1901223	biological_process	negative regulation of non-canonical NF-kappaB signal transduction

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN A 391

Chain	Residue
A	ASP60
A	ASP239
A	ASP282
A	HOH435
A	HOH553
A	HOH618

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN A 392

Chain	Residue
A	HOH416
A	HOH552
A	HOH553
A	ASP60
A	GLY61
A	HOH402

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site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 A 393

Chain	Residue
A	ASN188
A	ASP201
A	TYR202

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site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FLC A 394

Chain	Residue
A	ARG33
A	GLU37
A	HIS62
A	ALA63
A	ARG186
A	GLU300
A	LYS303
A	HOH416
A	HOH552

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Functional Information from PROSITE/UniProt

site_id	PS01032
Number of Residues	9
Details	PPM_1 PPM-type phosphatase domain signature. FFAVYDGHA

Chain	Residue	Details
A	PHE55-ALA63

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	268
Details	Domain: {"description":"PPM-type phosphatase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01082","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9003755","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A6Q","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Lipidation: {"description":"N-myristoyl glycine","evidences":[{"source":"PubMed","id":"20213681","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25255805","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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