Manganese in PDB 2gmv: Pepck Complex with A Gtp-Competitive Inhibitor

All present enzymatic activity of Pepck Complex with A Gtp-Competitive Inhibitor:
4.1.1.32;

The structure of Pepck Complex with A Gtp-Competitive Inhibitor, PDB code: 2gmv was solved by P.Dunten, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.31 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	128.011, 66.134, 137.360, 90.00, 145.09, 90.00
R / Rfree (%)	21.7 / 28.7

The structure of Pepck Complex with A Gtp-Competitive Inhibitor also contains other interesting chemical elements:

Fluorine

(F)

1 atom

The binding sites of Manganese atom in the Pepck Complex with A Gtp-Competitive Inhibitor (pdb code 2gmv). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Pepck Complex with A Gtp-Competitive Inhibitor, PDB code: 2gmv:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Pepck Complex with A Gtp-Competitive Inhibitor


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Pepck Complex with A Gtp-Competitive Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn701 b:42.3 occ:1.00 OD1 A:ASP311 2.3 24.1 1.0 NZ A:LYS244 2.4 22.5 1.0 NE2 A:HIS264 2.4 25.1 1.0 CG A:ASP311 3.1 26.1 1.0 CE1 A:HIS264 3.2 16.8 1.0 CE A:LYS244 3.3 17.2 1.0 OD2 A:ASP311 3.3 26.9 1.0 CD2 A:HIS264 3.3 23.2 1.0 O2P A:PEP702 3.8 31.2 1.0 O3P A:PEP702 4.2 29.0 1.0 ND1 A:HIS264 4.3 18.8 1.0 NZ A:LYS290 4.4 21.2 1.0 CG A:HIS264 4.4 21.3 1.0 CB A:ASP311 4.5 23.2 1.0 CD A:LYS244 4.6 22.4 1.0 P A:PEP702 4.7 28.9 1.0 CZ A:PHE485 4.9 18.1 1.0 CE1 A:PHE485 4.9 21.7 1.0

Manganese binding site 2 out of 2 in the Pepck Complex with A Gtp-Competitive Inhibitor


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Pepck Complex with A Gtp-Competitive Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn701 b:60.2 occ:1.00 OD1 B:ASP311 2.3 39.8 1.0 NZ B:LYS244 2.4 31.9 1.0 NE2 B:HIS264 2.6 39.8 1.0 CG B:ASP311 3.2 43.8 1.0 OD2 B:ASP311 3.3 41.8 1.0 CE1 B:HIS264 3.4 36.1 1.0 CE B:LYS244 3.4 29.0 1.0 CD2 B:HIS264 3.5 39.0 1.0 O2P B:PEP702 3.9 41.2 1.0 O3P B:PEP702 4.1 40.9 1.0 ND1 B:HIS264 4.5 34.6 1.0 CB B:ASP311 4.5 39.1 1.0 CG B:HIS264 4.5 37.8 1.0 P B:PEP702 4.7 44.0 1.0 CD B:LYS244 4.7 27.1 1.0 CE B:LYS290 4.8 46.7 1.0

S.L.Pietranico, L.H.Foley, N.Huby, W.Yun, P.Dunten, J.Vermeulen, P.Wang, K.Toth, G.Ramsey, M.L.Gubler, S.J.Wertheimer. C-8 Modifications of 3-Alkyl-1,8-Dibenzylxanthines As Inhibitors of Human Cytosolic Phosphoenolpyruvate Carboxykinase. Bioorg.Med.Chem.Lett. V. 17 3835 2007.
ISSN: ISSN 0960-894X
PubMed: 17532214
DOI: 10.1016/J.BMCL.2007.05.013