Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1KHB

PEPCK complex with nonhydrolyzable GTP analog, native data

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
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	0005739	cellular_component	mitochondrion
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	0010447	biological_process	response to acidic pH
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0016829	molecular_function	lyase activity
A	0016831	molecular_function	carboxy-lyase activity
A	0017076	molecular_function	purine nucleotide binding
A	0018105	biological_process	peptidyl-serine phosphorylation
A	0019543	biological_process	propionate catabolic process
A	0030145	molecular_function	manganese ion binding
A	0031406	molecular_function	carboxylic acid binding
A	0032868	biological_process	response to insulin
A	0032869	biological_process	cellular response to insulin stimulus
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	0070062	cellular_component	extracellular exosome
A	0070365	biological_process	hepatocyte differentiation
A	0071333	biological_process	cellular response to glucose stimulus
A	0071549	biological_process	cellular response to dexamethasone stimulus
A	0072350	biological_process	tricarboxylic acid metabolic process
A	0106264	molecular_function	protein serine kinase activity (using GTP as donor)

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN A 701

Chain	Residue
A	THR291
A	GCP704
A	HOH788
A	HOH804
A	HOH805

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN A 702

Chain	Residue
A	LYS244
A	HIS264
A	ASP311
A	GCP704

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT A 703

Chain	Residue
A	ARG87
A	TYR235
A	LYS244

site_id	AC4
Number of Residues	24
Details	BINDING SITE FOR RESIDUE GCP A 704

Chain	Residue
A	ALA287
A	GLY289
A	LYS290
A	THR291
A	ASN292
A	ASP311
A	VAL335
A	ARG405
A	ARG436
A	TRP516
A	PHE517
A	PHE525
A	GLY529
A	PHE530
A	ASN533
A	MN701
A	MN702
A	HOH731
A	HOH732
A	HOH737
A	HOH787
A	HOH788
A	HOH805
A	HOH845

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 705

Chain	Residue
A	SER449
A	TRP450
A	PRO509
A	LYS510
A	ILE511
A	HOH876
A	HOH923

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 706

Chain	Residue
A	TYR72
A	ILE348
A	GLN352
A	HOH733

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	1
Details	Active site: {"evidences":[{"source":"PubMed","id":"11851336","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32322062","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	11
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11851336","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14552798","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17532214","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P07379","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11851336","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine; by p300/EP300","evidences":[{"source":"PubMed","id":"20167786","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21726808","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by PKB/AKT1","evidences":[{"source":"PubMed","id":"32322062","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; by p300/EP300","evidences":[{"source":"PubMed","id":"30193097","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9Z2V4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q16822","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q16822","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P07379","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1aq2

Chain	Residue	Details
A	HIS264
A	LYS290
A	ARG405

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1aq2

Chain	Residue	Details
A	HIS264
A	ARG405

site_id	MCSA1
Number of Residues	8
Details	M-CSA 863

Chain	Residue	Details
A	ARG87	electrostatic stabiliser, enhance reactivity
A	TYR235	electrostatic stabiliser, steric role
A	LYS244	metal ligand
A	HIS264	metal ligand
A	SER286	electrostatic stabiliser
A	CYS288	metal ligand
A	ASP311	metal ligand
A	ARG405	electrostatic stabiliser, enhance reactivity

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