3LC6

The alternative conformation structure of isocitrate dehydrogenase kinase/phosphatase from E. Coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0004721	molecular_function	phosphoprotein phosphatase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006006	biological_process	glucose metabolic process
A	0006097	biological_process	glyoxylate cycle
A	0006099	biological_process	tricarboxylic acid cycle
A	0006470	biological_process	protein dephosphorylation
A	0008772	molecular_function	[isocitrate dehydrogenase (NADP+)] kinase activity
A	0016208	molecular_function	AMP binding
A	0016310	biological_process	phosphorylation
A	0016788	molecular_function	hydrolase activity, acting on ester bonds
A	0016791	molecular_function	phosphatase activity
A	0018105	biological_process	peptidyl-serine phosphorylation
A	0050790	biological_process	regulation of catalytic activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0004721	molecular_function	phosphoprotein phosphatase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006006	biological_process	glucose metabolic process
B	0006097	biological_process	glyoxylate cycle
B	0006099	biological_process	tricarboxylic acid cycle
B	0006470	biological_process	protein dephosphorylation
B	0008772	molecular_function	[isocitrate dehydrogenase (NADP+)] kinase activity
B	0016208	molecular_function	AMP binding
B	0016310	biological_process	phosphorylation
B	0016788	molecular_function	hydrolase activity, acting on ester bonds
B	0016791	molecular_function	phosphatase activity
B	0018105	biological_process	peptidyl-serine phosphorylation
B	0050790	biological_process	regulation of catalytic activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP A 1762

Chain	Residue
A	PRO316
A	GLU416
A	ARG417
A	MET419
A	PRO421
A	ASN462
A	TYR474
A	ASP475
A	MG579
A	ILE318
A	GLY320
A	MET321
A	VAL322
A	MET323
A	VAL325
A	VAL334
A	LYS336

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 579

Chain	Residue
A	LYS461
A	ASN462
A	ASP475
A	ADP1762

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site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE AMP B 1604

Chain	Residue
B	SER101
B	ASN104
B	SER105
B	HIS113
B	ILE123
B	LYS291
B	LYS294
B	THR295
B	PHE375
B	ASN377

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00747

Chain	Residue	Details
A	ALA370
B	ALA370
A	ASP371
B	ASP371

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00747

Chain	Residue	Details
A	GLU314
A	PHE335
B	GLU314
B	PHE335
A	ALA315
A	LYS336
B	ALA315
B	LYS336

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