Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4YWB

Structure of rat cytosolic pepck in complex with 3-mercaptopicolinic acid and oxalic acid

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
C	0000287	molecular_function	magnesium ion binding
C	0004550	molecular_function	nucleoside diphosphate kinase activity
C	0004611	molecular_function	phosphoenolpyruvate carboxykinase activity
C	0004613	molecular_function	phosphoenolpyruvate carboxykinase (GTP) activity
C	0005525	molecular_function	GTP binding
C	0005737	cellular_component	cytoplasm
C	0005783	cellular_component	endoplasmic reticulum
C	0005829	cellular_component	cytosol
C	0006006	biological_process	glucose metabolic process
C	0006094	biological_process	gluconeogenesis
C	0006107	biological_process	oxaloacetate metabolic process
C	0006629	biological_process	lipid metabolic process
C	0009617	biological_process	response to bacterium
C	0014823	biological_process	response to activity
C	0016301	molecular_function	kinase activity
C	0016831	molecular_function	carboxy-lyase activity
C	0017076	molecular_function	purine nucleotide binding
C	0018105	biological_process	peptidyl-serine phosphorylation
C	0019003	molecular_function	GDP binding
C	0019543	biological_process	propionate catabolic process
C	0030145	molecular_function	manganese ion binding
C	0031406	molecular_function	carboxylic acid binding
C	0031667	biological_process	response to nutrient levels
C	0032496	biological_process	response to lipopolysaccharide
C	0032868	biological_process	response to insulin
C	0032869	biological_process	cellular response to insulin stimulus
C	0033993	biological_process	response to lipid
C	0042593	biological_process	glucose homeostasis
C	0042594	biological_process	response to starvation
C	0043382	biological_process	positive regulation of memory T cell differentiation
C	0043648	biological_process	dicarboxylic acid metabolic process
C	0045944	biological_process	positive regulation of transcription by RNA polymerase II
C	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
C	0046327	biological_process	glycerol biosynthetic process from pyruvate
C	0046872	molecular_function	metal ion binding
C	0046889	biological_process	positive regulation of lipid biosynthetic process
C	0046890	biological_process	regulation of lipid biosynthetic process
C	0051365	biological_process	cellular response to potassium ion starvation
C	0070365	biological_process	hepatocyte differentiation
C	0070741	biological_process	response to interleukin-6
C	0071300	biological_process	cellular response to retinoic acid
C	0071320	biological_process	cellular response to cAMP
C	0071332	biological_process	cellular response to fructose stimulus
C	0071333	biological_process	cellular response to glucose stimulus
C	0071347	biological_process	cellular response to interleukin-1
C	0071356	biological_process	cellular response to tumor necrosis factor
C	0071377	biological_process	cellular response to glucagon stimulus
C	0071456	biological_process	cellular response to hypoxia
C	0071474	biological_process	cellular hyperosmotic response
C	0071475	biological_process	cellular hyperosmotic salinity response
C	0071476	biological_process	cellular hypotonic response
C	0071477	biological_process	cellular hypotonic salinity response
C	0071549	biological_process	cellular response to dexamethasone stimulus
C	0072350	biological_process	tricarboxylic acid metabolic process
C	0097403	biological_process	cellular response to raffinose
C	0106264	molecular_function	protein serine kinase activity (using GTP as donor)
C	1904628	biological_process	cellular response to phorbol 13-acetate 12-myristate
C	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 701

Chain	Residue
A	LYS244
A	HIS264
A	ASP311
A	OXD704
A	HOH1086

site_id	AC2
Number of Residues	5
Details	binding site for residue MN A 702

Chain	Residue
A	HOH1280
A	HIS502
A	GLU607
A	HOH947
A	HOH1134

site_id	AC3
Number of Residues	5
Details	binding site for residue NA A 703

Chain	Residue
A	LEU79
A	ASN208
A	HOH999
A	HOH1062
A	HOH1304

site_id	AC4
Number of Residues	11
Details	binding site for residue OXD A 704

Chain	Residue
A	ARG87
A	LYS244
A	HIS264
A	SER286
A	ASP311
A	ARG405
A	MN701
A	HOH923
A	HOH1063
A	HOH1086
A	HOH1099

site_id	AC5
Number of Residues	9
Details	binding site for residue 1WD A 705

Chain	Residue
A	PHE284
A	CYS288
A	GLY434
A	GLY435
A	ARG436
A	VAL514
A	ASN515
A	TRP516
A	PHE517

site_id	AC6
Number of Residues	3
Details	binding site for residue CL A 706

Chain	Residue
A	TYR235
A	GLY237
A	ASN403

site_id	AC7
Number of Residues	5
Details	binding site for residue MN C 701

Chain	Residue
C	LYS244
C	HIS264
C	ASP311
C	OXD704
C	HOH1140

site_id	AC8
Number of Residues	5
Details	binding site for residue MN C 702

Chain	Residue
C	HIS502
C	GLU607
C	HOH843
C	HOH1155
C	HOH1269

site_id	AC9
Number of Residues	5
Details	binding site for residue NA C 703

Chain	Residue
C	LEU79
C	ASN208
C	HOH1050
C	HOH1087
C	HOH1306

site_id	AD1
Number of Residues	11
Details	binding site for residue OXD C 704

Chain	Residue
C	ARG87
C	LYS244
C	HIS264
C	SER286
C	ASP311
C	ARG405
C	MN701
C	HOH935
C	HOH997
C	HOH1103
C	HOH1140

site_id	AD2
Number of Residues	9
Details	binding site for residue 1WD C 705

Chain	Residue
C	CYS288
C	GLY434
C	GLY435
C	ARG436
C	VAL514
C	ASN515
C	TRP516
C	PHE517
C	HOH1192

site_id	AD3
Number of Residues	4
Details	binding site for residue CL C 706

Chain	Residue
C	TYR235
C	GLY237
C	ASN403
C	HOH997

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
C	CYS288
A	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
C	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
C	TYR235
C	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
C	LYS244
C	HIS264
C	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
C	SER286
A	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
C	ALA287
C	ARG436
C	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
C	ARG405

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

Chain	Residue	Details
C	SER19
C	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
C	LYS71
C	LYS594
A	LYS70
A	LYS71
A	LYS594
C	LYS70

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

Chain	Residue	Details
A	SER90
C	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
C	LYS91

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

Chain	Residue	Details
A	THR178
C	THR178

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

Chain	Residue	Details
A	SER286
C	SER286

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

Chain	Residue	Details
A	LYS524
C	LYS473
C	LYS521
C	LYS524
A	LYS473
A	LYS521

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