Magnesium in PDB 1ayl: Phosphoenolpyruvate Carboxykinase

All present enzymatic activity of Phosphoenolpyruvate Carboxykinase:
4.1.1.49;

The structure of Phosphoenolpyruvate Carboxykinase, PDB code: 1ayl was solved by L.W.Tari, U.Pugazenthi, H.Goldie, L.T.J.Delbaere, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 1.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	127.510, 96.690, 46.960, 90.00, 96.63, 90.00
R / Rfree (%)	19.5 / 23.4

The binding sites of Magnesium atom in the Phosphoenolpyruvate Carboxykinase (pdb code 1ayl). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Phosphoenolpyruvate Carboxykinase, PDB code: 1ayl:

Magnesium binding site 1 out of 1 in the Phosphoenolpyruvate Carboxykinase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Phosphoenolpyruvate Carboxykinase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg543 b:20.3 occ:1.00 HG1 A:THR255 1.7 0.0 1.0 H2 A:HOH702 2.1 0.0 1.0 O3G A:ATP544 2.1 14.2 1.0 OG1 A:THR255 2.1 10.1 1.0 O A:HOH702 2.2 12.5 1.0 O2B A:ATP544 2.2 15.1 1.0 O A:HOH822 2.3 17.9 1.0 O A:HOH875 2.3 15.8 1.0 H1 A:HOH875 2.4 0.0 1.0 H2 A:HOH822 2.6 0.0 1.0 H1 A:HOH822 2.6 0.0 1.0 H1 A:HOH702 3.0 0.0 1.0 H2 A:HOH875 3.1 0.0 1.0 CB A:THR255 3.3 7.7 1.0 H1 A:HOH765 3.3 0.0 1.0 PG A:ATP544 3.3 12.5 1.0 PB A:ATP544 3.4 11.6 1.0 H1 A:HOH805 3.5 0.0 1.0 H A:THR255 3.5 0.0 1.0 O3B A:ATP544 3.6 14.9 1.0 O A:HOH765 3.9 18.9 1.0 O2A A:ATP544 3.9 13.6 1.0 O A:TYR286 3.9 11.0 1.0 H2 A:HOH765 3.9 0.0 1.0 OD2 A:ASP268 3.9 12.3 1.0 N A:THR255 4.0 9.3 1.0 O1G A:ATP544 4.1 15.0 1.0 O A:HOH805 4.1 23.3 1.0 CA A:THR255 4.2 10.0 1.0 O A:ASP268 4.3 10.6 1.0 OD1 A:ASP269 4.3 14.6 1.0 CG2 A:THR255 4.3 6.9 1.0 O3A A:ATP544 4.3 13.8 1.0 O2G A:ATP544 4.4 11.0 1.0 PA A:ATP544 4.5 14.0 1.0 O1B A:ATP544 4.5 14.0 1.0 H1 A:HOH551 4.6 0.0 1.0 HZ2 A:LYS254 4.6 0.0 1.0 HZ1 A:LYS254 4.8 0.0 1.0 CG A:ASP268 4.8 15.8 1.0 H2 A:HOH805 4.8 0.0 1.0 CB A:LYS254 4.9 10.4 1.0 O1A A:ATP544 4.9 15.2 1.0 C A:TYR286 4.9 10.8 1.0 CG A:ASP269 4.9 14.8 1.0 CE A:LYS254 5.0 11.0 1.0

L.W.Tari, A.Matte, U.Pugazhenthi, H.Goldie, L.T.Delbaere. Snapshot of An Enzyme Reaction Intermediate in the Structure of the Atp-MG2+-Oxalate Ternary Complex of Escherichia Coli Pep Carboxykinase. Nat.Struct.Biol. V. 3 355 1996.
ISSN: ISSN 1072-8368
PubMed: 8599762
DOI: 10.1038/NSB0496-355