Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2RK7

The Structure of rat cytosolic PEPCK in complex with oxalate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004550	molecular_function	nucleoside diphosphate kinase activity
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	0005783	cellular_component	endoplasmic reticulum
A	0005829	cellular_component	cytosol
A	0006006	biological_process	glucose metabolic process
A	0006094	biological_process	gluconeogenesis
A	0006107	biological_process	oxaloacetate metabolic process
A	0006629	biological_process	lipid metabolic process
A	0009617	biological_process	response to bacterium
A	0014823	biological_process	response to activity
A	0016301	molecular_function	kinase activity
A	0016831	molecular_function	carboxy-lyase activity
A	0017076	molecular_function	purine nucleotide binding
A	0018105	biological_process	peptidyl-serine phosphorylation
A	0019003	molecular_function	GDP binding
A	0019543	biological_process	propionate catabolic process
A	0030145	molecular_function	manganese ion binding
A	0031406	molecular_function	carboxylic acid binding
A	0031667	biological_process	response to nutrient levels
A	0032496	biological_process	response to lipopolysaccharide
A	0032868	biological_process	response to insulin
A	0032869	biological_process	cellular response to insulin stimulus
A	0033993	biological_process	response to lipid
A	0042593	biological_process	glucose homeostasis
A	0042594	biological_process	response to starvation
A	0043382	biological_process	positive regulation of memory T cell differentiation
A	0043648	biological_process	dicarboxylic acid metabolic process
A	0045944	biological_process	positive regulation of transcription by RNA polymerase II
A	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
A	0046327	biological_process	glycerol biosynthetic process from pyruvate
A	0046872	molecular_function	metal ion binding
A	0046889	biological_process	positive regulation of lipid biosynthetic process
A	0046890	biological_process	regulation of lipid biosynthetic process
A	0051365	biological_process	cellular response to potassium ion starvation
A	0070365	biological_process	hepatocyte differentiation
A	0070741	biological_process	response to interleukin-6
A	0071300	biological_process	cellular response to retinoic acid
A	0071320	biological_process	cellular response to cAMP
A	0071332	biological_process	cellular response to fructose stimulus
A	0071333	biological_process	cellular response to glucose stimulus
A	0071347	biological_process	cellular response to interleukin-1
A	0071356	biological_process	cellular response to tumor necrosis factor
A	0071377	biological_process	cellular response to glucagon stimulus
A	0071456	biological_process	cellular response to hypoxia
A	0071474	biological_process	cellular hyperosmotic response
A	0071475	biological_process	cellular hyperosmotic salinity response
A	0071476	biological_process	cellular hypotonic response
A	0071477	biological_process	cellular hypotonic salinity response
A	0071549	biological_process	cellular response to dexamethasone stimulus
A	0072350	biological_process	tricarboxylic acid metabolic process
A	0097403	biological_process	cellular response to raffinose
A	0106264	molecular_function	protein serine kinase activity (using GTP as donor)
A	1904628	biological_process	cellular response to phorbol 13-acetate 12-myristate
A	1904640	biological_process	response to methionine
B	0000287	molecular_function	magnesium ion binding
B	0004550	molecular_function	nucleoside diphosphate kinase activity
B	0004611	molecular_function	phosphoenolpyruvate carboxykinase activity
B	0004613	molecular_function	phosphoenolpyruvate carboxykinase (GTP) activity
B	0005525	molecular_function	GTP binding
B	0005737	cellular_component	cytoplasm
B	0005783	cellular_component	endoplasmic reticulum
B	0005829	cellular_component	cytosol
B	0006006	biological_process	glucose metabolic process
B	0006094	biological_process	gluconeogenesis
B	0006107	biological_process	oxaloacetate metabolic process
B	0006629	biological_process	lipid metabolic process
B	0009617	biological_process	response to bacterium
B	0014823	biological_process	response to activity
B	0016301	molecular_function	kinase activity
B	0016831	molecular_function	carboxy-lyase activity
B	0017076	molecular_function	purine nucleotide binding
B	0018105	biological_process	peptidyl-serine phosphorylation
B	0019003	molecular_function	GDP binding
B	0019543	biological_process	propionate catabolic process
B	0030145	molecular_function	manganese ion binding
B	0031406	molecular_function	carboxylic acid binding
B	0031667	biological_process	response to nutrient levels
B	0032496	biological_process	response to lipopolysaccharide
B	0032868	biological_process	response to insulin
B	0032869	biological_process	cellular response to insulin stimulus
B	0033993	biological_process	response to lipid
B	0042593	biological_process	glucose homeostasis
B	0042594	biological_process	response to starvation
B	0043382	biological_process	positive regulation of memory T cell differentiation
B	0043648	biological_process	dicarboxylic acid metabolic process
B	0045944	biological_process	positive regulation of transcription by RNA polymerase II
B	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
B	0046327	biological_process	glycerol biosynthetic process from pyruvate
B	0046872	molecular_function	metal ion binding
B	0046889	biological_process	positive regulation of lipid biosynthetic process
B	0046890	biological_process	regulation of lipid biosynthetic process
B	0051365	biological_process	cellular response to potassium ion starvation
B	0070365	biological_process	hepatocyte differentiation
B	0070741	biological_process	response to interleukin-6
B	0071300	biological_process	cellular response to retinoic acid
B	0071320	biological_process	cellular response to cAMP
B	0071332	biological_process	cellular response to fructose stimulus
B	0071333	biological_process	cellular response to glucose stimulus
B	0071347	biological_process	cellular response to interleukin-1
B	0071356	biological_process	cellular response to tumor necrosis factor
B	0071377	biological_process	cellular response to glucagon stimulus
B	0071456	biological_process	cellular response to hypoxia
B	0071474	biological_process	cellular hyperosmotic response
B	0071475	biological_process	cellular hyperosmotic salinity response
B	0071476	biological_process	cellular hypotonic response
B	0071477	biological_process	cellular hypotonic salinity response
B	0071549	biological_process	cellular response to dexamethasone stimulus
B	0072350	biological_process	tricarboxylic acid metabolic process
B	0097403	biological_process	cellular response to raffinose
B	0106264	molecular_function	protein serine kinase activity (using GTP as donor)
B	1904628	biological_process	cellular response to phorbol 13-acetate 12-myristate
B	1904640	biological_process	response to methionine

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN A 700

Chain	Residue
A	LYS244
A	HIS264
A	ASP311
A	OXL5575
A	HOH5887

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA A 701

Chain	Residue
A	HOH6093
A	LEU79
A	ASN208
A	HOH5645
A	HOH5865

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE OXL A 5575

Chain	Residue
A	ARG87
A	LYS244
A	HIS264
A	SER286
A	ASP311
A	ARG405
A	MN700
A	HOH5673
A	HOH6044

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MN A 5576

Chain	Residue
A	PHE530
A	ASN533

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN B 700

Chain	Residue
B	LYS244
B	HIS264
B	ASP311
B	OXL5575
B	HOH5794

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA B 701

Chain	Residue
B	VAL65
B	LEU79
B	ASN208
B	HOH5645
B	HOH5726
B	HOH5939

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE OXL B 5575

Chain	Residue
B	ARG87
B	LYS244
B	HIS264
B	SER286
B	ASP311
B	ARG405
B	MN700
B	HOH5770
B	HOH5794

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MN B 5576

Chain	Residue
B	PHE530
B	ASN533

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE284-ASN292

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000269\|PubMed:23127136, ECO:0000269\|PubMed:2909519

Chain	Residue	Details
A	CYS288
B	CYS288

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:17685635, ECO:0000269\|PubMed:18772387, ECO:0000269\|PubMed:20476774, ECO:0000269\|PubMed:23127136, ECO:0000269\|PubMed:24863970

Chain	Residue	Details
A	ARG87
B	ARG87

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:18197707, ECO:0000269\|PubMed:18772387, ECO:0000269\|PubMed:20476774, ECO:0000269\|PubMed:23127136, ECO:0000269\|PubMed:24863970

Chain	Residue	Details
A	TYR235
A	ASN403
B	TYR235
B	ASN403

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:17685635, ECO:0000269\|PubMed:18197707, ECO:0000269\|PubMed:18772387, ECO:0000269\|PubMed:20476774, ECO:0000269\|PubMed:23127136, ECO:0000269\|PubMed:24863970, ECO:0000269\|PubMed:26322521, ECO:0000269\|PubMed:26709450, ECO:0000269\|PubMed:28345895, ECO:0000269\|PubMed:31461616, ECO:0007744\|PDB:4YW9, ECO:0007744\|PDB:5FH0, ECO:0007744\|PDB:5FH1, ECO:0007744\|PDB:5FH2, ECO:0007744\|PDB:5FH3, ECO:0007744\|PDB:5FH4, ECO:0007744\|PDB:5FH5, ECO:0007744\|PDB:5V97, ECO:0007744\|PDB:5V9F, ECO:0007744\|PDB:5V9G, ECO:0007744\|PDB:6P5O

Chain	Residue	Details
A	ASP311
B	LYS244
B	HIS264
B	ASP311
A	LYS244
A	HIS264

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:17685635, ECO:0000269\|PubMed:18197707, ECO:0000269\|PubMed:18772387, ECO:0000269\|PubMed:20476774, ECO:0000269\|PubMed:23127136, ECO:0000269\|PubMed:24863970

Chain	Residue	Details
A	SER286
B	SER286

site_id	SWS_FT_FI6
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:17685635, ECO:0000269\|PubMed:18772387, ECO:0000269\|PubMed:20476774, ECO:0000269\|PubMed:23127136, ECO:0000269\|PubMed:24863970, ECO:0000269\|PubMed:26322521, ECO:0000269\|PubMed:26709450, ECO:0000269\|PubMed:28345895, ECO:0007744\|PDB:4YW9, ECO:0007744\|PDB:5FH0, ECO:0007744\|PDB:5FH1, ECO:0007744\|PDB:5FH2, ECO:0007744\|PDB:5FH3, ECO:0007744\|PDB:5FH4, ECO:0007744\|PDB:5V97, ECO:0007744\|PDB:5V9F, ECO:0007744\|PDB:5V9G

Chain	Residue	Details
A	PHE530
B	ALA287
B	ARG436
B	PHE530
A	ALA287
A	ARG436

site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:17685635, ECO:0000269\|PubMed:20476774, ECO:0000269\|PubMed:23127136, ECO:0000269\|PubMed:24863970, ECO:0000269\|PubMed:26322521, ECO:0000269\|PubMed:26709450, ECO:0000269\|PubMed:28345895, ECO:0007744\|PDB:4YW9, ECO:0007744\|PDB:5FH0, ECO:0007744\|PDB:5FH1, ECO:0007744\|PDB:5FH2, ECO:0007744\|PDB:5FH3, ECO:0007744\|PDB:5FH4, ECO:0007744\|PDB:5V97, ECO:0007744\|PDB:5V9F, ECO:0007744\|PDB:5V9G

Chain	Residue	Details
A	ARG405
B	ARG405

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:22673903

Chain	Residue	Details
B	SER19
B	SER118
A	SER19
A	SER118

site_id	SWS_FT_FI9
Number of Residues	6
Details	MOD_RES: N6-acetyllysine; by p300/EP300 => ECO:0000250\|UniProtKB:P35558

Chain	Residue	Details
B	LYS71
B	LYS594
A	LYS70
A	LYS71
A	LYS594
B	LYS70

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P35558

Chain	Residue	Details
A	SER90
B	SER90

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: N6-acetyllysine; by p300/EP300 => ECO:0000250\|UniProtKB:P35558, ECO:0000269\|PubMed:30193097

Chain	Residue	Details
A	LYS91
B	LYS91

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:Q16822

Chain	Residue	Details
A	THR178
B	THR178

site_id	SWS_FT_FI13
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:Q16822

Chain	Residue	Details
A	SER286
B	SER286

site_id	SWS_FT_FI14
Number of Residues	6
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:30193097

Chain	Residue	Details
A	LYS524
B	LYS473
B	LYS521
B	LYS524
A	LYS473
A	LYS521

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)