4WIE

Crystal structure of apo-PEPCK from Mycobacterium tuberculosis with glycerol

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004611	molecular_function	phosphoenolpyruvate carboxykinase activity
A	0004613	molecular_function	phosphoenolpyruvate carboxykinase (GTP) activity
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006094	biological_process	gluconeogenesis
A	0016831	molecular_function	carboxy-lyase activity
A	0017076	molecular_function	purine nucleotide binding
A	0019543	biological_process	propionate catabolic process
A	0030145	molecular_function	manganese ion binding
A	0033993	biological_process	response to lipid
A	0042594	biological_process	response to starvation
A	0046327	biological_process	glycerol biosynthetic process from pyruvate
A	0046872	molecular_function	metal ion binding
A	0071333	biological_process	cellular response to glucose stimulus

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue MN A 701

Chain	Residue
A	LYS229
A	HIS249
A	LYS275
A	ASP296
A	HOH1409

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site_id	AC2
Number of Residues	8
Details	binding site for residue GOL A 702

Chain	Residue
A	ASN101
A	ARG234
A	PRO468
A	HOH1060
A	THR86
A	ILE88
A	THR99
A	ASN100

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Functional Information from PROSITE/UniProt

site_id	PS00505
Number of Residues	9
Details	PEPCK_GTP Phosphoenolpyruvate carboxykinase (GTP) signature. FPSACGKTN

Chain	Residue	Details
A	PHE269-ASN277

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P07379, ECO:0000255|HAMAP-Rule:MF_00452

Chain	Residue	Details
A	CYS273

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site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00452, ECO:0000269|Ref.2

Chain	Residue	Details
A	ARG81
A	LYS229
A	HIS249
A	ASP296
A	ASN387

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site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P07379, ECO:0000255|HAMAP-Rule:MF_00452

Chain	Residue	Details
A	TYR220
A	SER271
A	ALA272
A	ARG389
A	ARG420
A	PHE515

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