2IQ1

Crystal structure of human PPM1K

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004722	molecular_function	protein serine/threonine phosphatase activity
A	0006470	biological_process	protein dephosphorylation
A	0043169	molecular_function	cation binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 1

Chain	Residue
A	ASP127
A	GLY128
A	ASP337
A	HOH470
A	HOH472
A	HOH473

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	TYR122-GLY130

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22291014","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4DA1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22291014","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2IQ1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8BXN7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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