Potassium in PDB 2fpg: Crystal Structure of Pig Gtp-Specific Succinyl-Coa Synthetase in Complex with Gdp

All present enzymatic activity of Crystal Structure of Pig Gtp-Specific Succinyl-Coa Synthetase in Complex with Gdp:
6.2.1.4;

The structure of Crystal Structure of Pig Gtp-Specific Succinyl-Coa Synthetase in Complex with Gdp, PDB code: 2fpg was solved by M.E.Fraser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	115.86 / 2.96
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	133.780, 133.780, 73.090, 90.00, 90.00, 120.00
R / Rfree (%)	20.1 / 27.5

The binding sites of Potassium atom in the Crystal Structure of Pig Gtp-Specific Succinyl-Coa Synthetase in Complex with Gdp (pdb code 2fpg). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Crystal Structure of Pig Gtp-Specific Succinyl-Coa Synthetase in Complex with Gdp, PDB code: 2fpg:

Potassium binding site 1 out of 1 in the Crystal Structure of Pig Gtp-Specific Succinyl-Coa Synthetase in Complex with Gdp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of Pig Gtp-Specific Succinyl-Coa Synthetase in Complex with Gdp within 5.0Å range: probe atom residue distance (Å) B Occ B:K396 b:76.1 occ:1.00 OD2 B:ASP220 2.6 42.7 1.0 O3B B:GDP397 2.9 72.0 1.0 O1A B:GDP397 3.0 77.5 1.0 O B:ASN206 3.2 23.7 1.0 NZ B:LYS222 3.5 28.2 1.0 O2A B:GDP397 3.5 77.5 1.0 PA B:GDP397 3.5 78.4 1.0 O3A B:GDP397 3.6 75.5 1.0 CG B:ASP220 3.6 41.4 1.0 PB B:GDP397 3.9 72.0 1.0 CE B:LYS222 4.0 28.9 1.0 CB B:ASP220 4.1 38.9 1.0 C B:ASN206 4.3 23.6 1.0 CB B:ASN206 4.4 25.4 1.0 CD B:LYS222 4.5 25.8 1.0 OD1 B:ASP220 4.6 42.3 1.0 O1B B:GDP397 4.8 70.1 1.0 CA B:ASN206 4.8 24.1 1.0 CG B:ASN206 5.0 28.4 1.0

M.E.Fraser, K.Hayakawa, M.S.Hume, D.G.Ryan, E.R.Brownie. Interactions of Gtp with the Atp-Grasp Domain of Gtp-Specific Succinyl-Coa Synthetase J.Biol.Chem. V. 281 11058 2006.
ISSN: ISSN 0021-9258
PubMed: 16481318
DOI: 10.1074/JBC.M511785200