2IF8

Crystal structure of Inositol Phosphate Multikinase Ipk2 in complex with ADP and Mn2+ from S. cerevisiae

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0000166	molecular_function	nucleotide binding
A	0000823	molecular_function	inositol-1,4,5-trisphosphate 6-kinase activity
A	0000824	molecular_function	inositol-1,4,5,6-tetrakisphosphate 3-kinase activity
A	0000825	molecular_function	inositol-1,3,4,5-tetrakisphosphate 6-kinase activity
A	0000827	molecular_function	inositol-1,3,4,5,6-pentakisphosphate kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0006525	biological_process	arginine metabolic process
A	0008440	molecular_function	inositol-1,4,5-trisphosphate 3-kinase activity
A	0016236	biological_process	macroautophagy
A	0016301	molecular_function	kinase activity
A	0016303	molecular_function	1-phosphatidylinositol-3-kinase activity
A	0016740	molecular_function	transferase activity
A	0030674	molecular_function	protein-macromolecule adaptor activity
A	0032958	biological_process	inositol phosphate biosynthetic process
A	0036092	biological_process	phosphatidylinositol-3-phosphate biosynthetic process
A	0045944	biological_process	positive regulation of transcription by RNA polymerase II
A	0046854	biological_process	phosphatidylinositol phosphate biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0046934	molecular_function	1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity
A	0050821	biological_process	protein stabilization
A	0090575	cellular_component	RNA polymerase II transcription regulator complex
A	1900079	biological_process	regulation of arginine biosynthetic process
B	0000122	biological_process	negative regulation of transcription by RNA polymerase II
B	0000166	molecular_function	nucleotide binding
B	0000823	molecular_function	inositol-1,4,5-trisphosphate 6-kinase activity
B	0000824	molecular_function	inositol-1,4,5,6-tetrakisphosphate 3-kinase activity
B	0000825	molecular_function	inositol-1,3,4,5-tetrakisphosphate 6-kinase activity
B	0000827	molecular_function	inositol-1,3,4,5,6-pentakisphosphate kinase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0006525	biological_process	arginine metabolic process
B	0008440	molecular_function	inositol-1,4,5-trisphosphate 3-kinase activity
B	0016236	biological_process	macroautophagy
B	0016301	molecular_function	kinase activity
B	0016303	molecular_function	1-phosphatidylinositol-3-kinase activity
B	0016740	molecular_function	transferase activity
B	0030674	molecular_function	protein-macromolecule adaptor activity
B	0032958	biological_process	inositol phosphate biosynthetic process
B	0036092	biological_process	phosphatidylinositol-3-phosphate biosynthetic process
B	0045944	biological_process	positive regulation of transcription by RNA polymerase II
B	0046854	biological_process	phosphatidylinositol phosphate biosynthetic process
B	0046872	molecular_function	metal ion binding
B	0046934	molecular_function	1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity
B	0050821	biological_process	protein stabilization
B	0090575	cellular_component	RNA polymerase II transcription regulator complex
B	1900079	biological_process	regulation of arginine biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN A 402

Chain	Residue
A	LYS133
A	ASP325
A	ADP401

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA A 403

Chain	Residue
A	HOH556
A	GLU271
A	ASN274
A	GLY334
A	HOH424
A	HOH436
A	HOH540

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site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ADP A 401

Chain	Residue
A	LYS31
A	PRO67
A	GLU118
A	ASN119
A	LEU120
A	ASP131
A	ASP325
A	MN402
A	HOH603

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17050532","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2IF8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17050532","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2IEW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IF8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17050532","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2IEW","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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