Het-PDB Navi2 (PDB: 1AYL)

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Ligands
Code	Name	Link
ATP	Adenosine-5'-triphosphate	PoSSuM
MG	Magnesium ion	PoSSuM
OXL	Oxalate ion	PoSSuM

Non-standard Residues
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Glycosylation
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Download interaction data: 1AYL

Code :

1AYL PDBj RCSB PDB PDBe

Header :

KINASE (TRANSPHOSPHORYLATING)

Title :

PHOSPHOENOLPYRUVATE CARBOXYKINASE

Release Data :

1997-01-11

Compound :

mol_id	molecule	chains	synonym
1	PHOSPHOENOLPYRUVATE CARBOXYKINASE	A	ATP-OXALOACETATE CARBOXY-LYASE (ATP)
	ec: 4.1.1.49 other_details: ORDERED MAGNESIUM ION OBSERVED BOUND TO ATP

Source :

mol_id	organism_scientific
1	Escherichia coli (taxid:83333)
	strain: K12

Authors :

Tari, L.W., Pugazenthi, U., Goldie, H., Delbaere, L.T.J.

Keywords :

P-LOOP, PROTEIN-ATP COMPLEX, NUCLEOTIDE-TRIPHOSPHATE HYDROLASE, KINASE (TRANSPHOSPHORYLATING)

Exp. method :

X-RAY DIFFRACTION ( 1.8 Å )

Citation :

Snapshot of an enzyme reaction intermediate in the structure of the ATP-Mg2+-oxalate ternary complex of Escherichia coli PEP carboxykinase.

Tari, L.W.,Matte, A.,Pugazhenthi, U. et al.
(1996) Nat.Struct.Biol. 3 : 355 - 363

PubMed: 8599762
DOI: 10.1038/nsb0496-355

Allosteric Control by Calcium and Mechanism of Desensitization of Phosphoenolpyruvate Carboxykinase of Escherichia Coli

Goldie, H.,Sanwal, B.D.
To be Published

Crystal Structure of Escherichia Coli Phosphoenolpyruvate Carboxykinase: A New Structural Family with the P-Loop Nucleoside Triphosphate Hydrolase Fold

Matte, A.,Goldie, H.,Sweet, R.M. et al.
(1996) J.Mol.Biol. 256 : 126

Crystallization of the Calcium-Activated Phosphoenolpyruvate Carboxykinase from Escherichia Coli K12

Delbaere, L.T.,Vandonselaar, M.,Glaeske, D. et al.
(1991) J.Mol.Biol. 219 : 593

Sequence of the Pcka Gene of Escherichia Coli K-12: Relevance to Genetic and Allosteric Regulation and Homology of E. Coli Phosphoenolpyruvate Carboxykinase with the Enzymes from Trypanosoma Brucei and Saccharomyces Cerevisiae

Medina, V.,Pontarollo, R.,Glaeske, D. et al.
(1990) J.Bacteriol. 172 : 7151

Chain :

UniProt :

P22259 (PCKA_ECOLI)

Reaction:	EC:	Evidence:
Reaction:	Physiological Direction:	Evidence:
ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate	4.1.1.49	HAMAP-Rule:MF_00453, PubMed:6986370
ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate	-	HAMAP-Rule:MF_00453, PubMed:6986370

PDB ID: 1AYL

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Structure summary

Reaction