Manganese in PDB 3moe: The Structure of Rat Cytosolic Pepck Mutant A467G in Complex with Beta-Sulfopyruvate and Gtp

All present enzymatic activity of The Structure of Rat Cytosolic Pepck Mutant A467G in Complex with Beta-Sulfopyruvate and Gtp:
4.1.1.32;

The structure of The Structure of Rat Cytosolic Pepck Mutant A467G in Complex with Beta-Sulfopyruvate and Gtp, PDB code: 3moe was solved by T.A.Johnson, T.Holyoak, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.57 / 1.25
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.324, 119.117, 60.053, 90.00, 111.19, 90.00
R / Rfree (%)	14.8 / 17.4

The structure of The Structure of Rat Cytosolic Pepck Mutant A467G in Complex with Beta-Sulfopyruvate and Gtp also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Manganese atom in the The Structure of Rat Cytosolic Pepck Mutant A467G in Complex with Beta-Sulfopyruvate and Gtp (pdb code 3moe). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the The Structure of Rat Cytosolic Pepck Mutant A467G in Complex with Beta-Sulfopyruvate and Gtp, PDB code: 3moe:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the The Structure of Rat Cytosolic Pepck Mutant A467G in Complex with Beta-Sulfopyruvate and Gtp


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of The Structure of Rat Cytosolic Pepck Mutant A467G in Complex with Beta-Sulfopyruvate and Gtp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn700 b:10.0 occ:1.00 OD1 A:ASP311 2.1 5.9 1.0 O2G A:GTP1100 2.2 9.5 1.0 O1 A:SPV1200 2.2 11.1 1.0 NZ A:LYS244 2.3 6.6 1.0 O2 A:SPV1200 2.3 10.5 1.0 NE2 A:HIS264 2.3 5.7 1.0 C1 A:SPV1200 2.9 10.5 1.0 C2 A:SPV1200 3.0 11.1 1.0 CG A:ASP311 3.1 5.1 1.0 CD2 A:HIS264 3.2 4.6 1.0 CE1 A:HIS264 3.3 4.7 1.0 CE A:LYS244 3.3 4.7 1.0 OD2 A:ASP311 3.3 6.5 1.0 PG A:GTP1100 3.4 9.9 1.0 O3G A:GTP1100 3.8 10.6 1.0 NZ A:LYS290 4.0 6.3 1.0 O1G A:GTP1100 4.0 10.3 1.0 CE A:LYS290 4.1 5.5 1.0 O2' A:SPV1200 4.2 11.8 1.0 O A:HOH716 4.2 6.5 1.0 O A:HOH636 4.3 8.0 1.0 OG A:SER286 4.3 18.5 0.6 ND1 A:HIS264 4.4 4.9 1.0 CG A:HIS264 4.4 4.9 1.0 CB A:ASP311 4.5 5.1 1.0 C3 A:SPV1200 4.5 11.4 1.0 O3B A:GTP1100 4.7 9.7 1.0 CD A:LYS244 4.7 5.3 1.0 CB A:SER286 4.8 7.6 0.4 O A:ASP311 4.9 5.8 1.0 CZ A:PHE485 5.0 5.4 1.0

Manganese binding site 2 out of 2 in the The Structure of Rat Cytosolic Pepck Mutant A467G in Complex with Beta-Sulfopyruvate and Gtp


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of The Structure of Rat Cytosolic Pepck Mutant A467G in Complex with Beta-Sulfopyruvate and Gtp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn701 b:10.4 occ:1.00 O1G A:GTP1100 2.1 10.3 1.0 O A:HOH712 2.2 6.4 1.0 O2B A:GTP1100 2.2 10.1 1.0 O A:HOH716 2.2 6.5 1.0 OG1 A:THR291 2.3 5.3 1.0 O A:HOH684 2.3 6.3 1.0 PG A:GTP1100 3.3 9.9 1.0 PB A:GTP1100 3.3 10.1 1.0 CB A:THR291 3.4 4.5 1.0 O3B A:GTP1100 3.5 9.7 1.0 OD2 A:ASP310 3.8 6.6 1.0 O2G A:GTP1100 4.0 9.5 1.0 N A:THR291 4.0 5.1 1.0 O1A A:GTP1100 4.0 11.8 1.0 O A:HOH636 4.1 8.0 1.0 CA A:THR291 4.3 6.5 1.0 O A:ASP310 4.4 5.9 1.0 NH1 A:ARG405 4.4 4.5 1.0 O3A A:GTP1100 4.4 10.9 1.0 O1B A:GTP1100 4.4 9.9 1.0 CG2 A:THR291 4.4 8.3 1.0 CA A:GLY334 4.4 4.9 1.0 CG A:ASP310 4.5 6.0 1.0 O3G A:GTP1100 4.5 10.6 1.0 OD1 A:ASP311 4.5 5.9 1.0 O A:PHE333 4.6 5.7 1.0 O A:HOH691 4.7 6.2 1.0 N A:VAL335 4.8 5.0 1.0 PA A:GTP1100 4.8 11.3 1.0 CB A:LYS290 5.0 6.1 1.0

T.A.Johnson, T.Holyoak. Increasing the Conformational Entropy of the Omega-Loop Lid Domain in Phosphoenolpyruvate Carboxykinase Impairs Catalysis and Decreases Catalytic Fidelity . Biochemistry V. 49 5176 2010.
ISSN: ISSN 0006-2960
PubMed: 20476774
DOI: 10.1021/BI100399E