Magnesium in PDB 2one: Asymmetric Yeast Enolase Dimer Complexed with Resolved 2'- Phosphoglycerate and Phosphoenolpyruvate

All present enzymatic activity of Asymmetric Yeast Enolase Dimer Complexed with Resolved 2'- Phosphoglycerate and Phosphoenolpyruvate:
4.2.1.11;

The structure of Asymmetric Yeast Enolase Dimer Complexed with Resolved 2'- Phosphoglycerate and Phosphoenolpyruvate, PDB code: 2one was solved by L.Lebioda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	9.00 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	63.100, 110.000, 66.200, 90.00, 113.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Magnesium atom in the Asymmetric Yeast Enolase Dimer Complexed with Resolved 2'- Phosphoglycerate and Phosphoenolpyruvate (pdb code 2one). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Asymmetric Yeast Enolase Dimer Complexed with Resolved 2'- Phosphoglycerate and Phosphoenolpyruvate, PDB code: 2one:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Asymmetric Yeast Enolase Dimer Complexed with Resolved 2'- Phosphoglycerate and Phosphoenolpyruvate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Asymmetric Yeast Enolase Dimer Complexed with Resolved 2'- Phosphoglycerate and Phosphoenolpyruvate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg450 b:26.9 occ:0.86 OE2 A:GLU295 1.9 16.9 1.0 O2 A:2PG441 2.0 23.0 1.0 OD2 A:ASP246 2.2 22.9 1.0 OD2 A:ASP320 2.3 13.2 1.0 O A:HOH576 2.3 17.4 1.0 O1 A:2PG441 2.6 22.4 1.0 C1 A:2PG441 2.7 22.6 1.0 CG A:ASP246 3.0 22.5 1.0 CD A:GLU295 3.0 14.6 1.0 OD1 A:ASP246 3.2 17.6 1.0 CG A:ASP320 3.3 16.2 1.0 NZ A:LYS396 3.4 10.0 1.0 OE1 A:GLU295 3.6 15.0 1.0 CB A:ASP320 3.7 15.5 1.0 LI A:LI451 3.8 16.0 1.0 CD2 A:LEU343 3.8 10.0 1.0 CG A:GLU295 4.0 14.1 1.0 C2 A:2PG441 4.1 23.1 1.0 NE2 A:GLN167 4.2 23.2 1.0 O A:HOH604 4.2 24.2 1.0 NZ A:LYS345 4.2 13.0 1.0 CB A:ASP246 4.3 19.4 1.0 OD1 A:ASP320 4.4 19.7 1.0 CE A:LYS396 4.5 10.0 1.0 OD2 A:ASP296 4.5 12.0 1.0 OE2 A:GLU168 4.8 20.6 1.0 O A:HOH568 4.8 18.8 0.9 C3 A:2PG441 4.9 23.1 1.0 CE A:LYS345 4.9 17.3 1.0

Magnesium binding site 2 out of 2 in the Asymmetric Yeast Enolase Dimer Complexed with Resolved 2'- Phosphoglycerate and Phosphoenolpyruvate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Asymmetric Yeast Enolase Dimer Complexed with Resolved 2'- Phosphoglycerate and Phosphoenolpyruvate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg460 b:25.7 occ:0.91 OD2 B:ASP246 1.9 23.3 1.0 OE2 B:GLU295 2.0 21.6 1.0 OD2 B:ASP320 2.1 17.7 1.0 O B:HOH628 2.2 10.0 0.7 O1 B:PEP440 2.4 28.8 1.0 O2' B:PEP440 2.4 28.4 1.0 C1 B:PEP440 2.7 27.2 1.0 CG B:ASP246 3.0 25.5 1.0 CD B:GLU295 3.0 20.2 1.0 CG B:ASP320 3.2 20.4 1.0 OD1 B:ASP246 3.4 25.6 1.0 OE1 B:GLU295 3.8 21.2 1.0 NZ B:LYS396 3.8 19.9 1.0 CB B:ASP320 4.0 20.6 1.0 NZ B:LYS345 4.0 23.0 1.0 CD2 B:LEU343 4.1 16.5 1.0 CG B:GLU295 4.1 19.3 1.0 C2 B:PEP440 4.2 27.4 1.0 OD1 B:ASP320 4.2 21.7 1.0 OE2 B:GLU168 4.3 24.9 1.0 CB B:ASP246 4.4 21.0 1.0 OD2 B:ASP296 4.5 26.9 1.0 CE B:LYS396 4.7 19.2 1.0 O2 B:PEP440 4.9 27.1 1.0

E.Zhang, J.M.Brewer, W.Minor, L.A.Carreira, L.Lebioda. Mechanism of Enolase: the Crystal Structure of Asymmetric Dimer Enolase-2-Phospho-D-Glycerate/Enolase- Phosphoenolpyruvate at 2.0 A Resolution. Biochemistry V. 36 12526 1997.
ISSN: ISSN 0006-2960
PubMed: 9376357
DOI: 10.1021/BI9712450