Potassium in PDB 3bol: Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+

All present enzymatic activity of Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+:
2.1.1.13;

The structure of Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+, PDB code: 3bol was solved by M.Koutmos, J.L.Smith, M.L.Ludwig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.62 / 1.85
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	59.626, 85.841, 125.587, 90.00, 100.67, 90.00
R / Rfree (%)	19.3 / 22.8

The structure of Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+ also contains other interesting chemical elements:

Yttrium	(Y)	1 atom
Zinc	(Zn)	3 atoms

The binding sites of Potassium atom in the Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+ (pdb code 3bol). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+, PDB code: 3bol:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:K703 b:18.0 occ:1.00 O A:GLY271 2.7 14.9 1.0 OE1 A:GLU232 2.8 16.2 1.0 O A:HOH745 2.8 23.2 1.0 O A:GLY20 2.8 14.9 1.0 OD2 A:ASP19 2.8 14.0 1.0 O A:ASP19 2.9 14.6 1.0 C A:ASP19 3.4 15.2 1.0 C A:GLY20 3.6 15.9 1.0 N A:GLY20 3.9 15.5 1.0 CG A:ASP19 3.9 14.8 1.0 CA A:GLY20 3.9 15.3 1.0 CD1 A:LEU62 3.9 21.3 1.0 CD A:GLU232 3.9 15.3 1.0 C A:GLY271 3.9 16.2 1.0 CA A:ASP19 4.3 14.4 1.0 O A:HOH958 4.3 27.2 1.0 N A:ASP19 4.4 13.9 1.0 N A:GLY271 4.5 14.1 1.0 OE2 A:GLU146 4.6 18.9 1.0 CG A:LEU62 4.6 16.9 1.0 N A:ALA21 4.6 16.1 1.0 CB A:ASP19 4.6 13.3 1.0 CG A:GLU232 4.7 14.7 1.0 OD1 A:ASP19 4.7 16.5 1.0 OE2 A:GLU232 4.7 17.1 1.0 CA A:GLY271 4.8 14.0 1.0 N A:CYS272 4.9 16.3 1.0 CA A:CYS272 4.9 15.8 1.0

Potassium binding site 2 out of 2 in the Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Cobalamin-Dependent Methionine Synthase (1-566) From Thermotoga Maritima Complexed with ZN2+ within 5.0Å range: probe atom residue distance (Å) B Occ B:K704 b:20.0 occ:1.00 O B:GLY271 2.6 22.4 1.0 O B:HOH790 2.6 24.6 1.0 OE1 B:GLU232 2.7 19.5 1.0 O B:GLY20 2.8 21.4 1.0 OD2 B:ASP19 2.8 22.4 1.0 O B:ASP19 2.9 20.2 1.0 C B:ASP19 3.4 21.3 1.0 C B:GLY20 3.5 21.2 1.0 CD1 B:LEU62 3.7 26.8 1.0 C B:GLY271 3.9 22.5 1.0 CD B:GLU232 3.9 21.7 1.0 CA B:GLY20 3.9 20.8 1.0 N B:GLY20 3.9 21.6 1.0 CG B:ASP19 3.9 22.7 1.0 CA B:ASP19 4.3 21.3 1.0 N B:GLY271 4.4 21.2 1.0 N B:ASP19 4.4 21.5 1.0 OE2 B:GLU146 4.5 20.4 1.0 CG B:LEU62 4.5 20.2 1.0 N B:ALA21 4.5 20.4 1.0 CB B:ASP19 4.6 21.0 1.0 CG B:GLU232 4.6 21.4 1.0 OE2 B:GLU232 4.7 22.2 1.0 CA B:GLY271 4.7 21.5 1.0 N B:CYS272 4.8 22.5 1.0 CA B:CYS272 4.8 24.1 1.0 OD1 B:ASP19 4.8 18.6 1.0 OXT B:HCS710 4.9 23.4 0.7 CD2 B:LEU18 5.0 21.1 1.0 CB B:GLU232 5.0 21.3 1.0

M.Koutmos, R.Pejchal, T.M.Bomer, R.G.Matthews, J.L.Smith, M.L.Ludwig. Metal Active Site Elasticity Linked to Activation of Homocysteine in Methionine Synthases. Proc.Natl.Acad.Sci.Usa V. 105 3286 2008.
ISSN: ISSN 0027-8424
PubMed: 18296644
DOI: 10.1073/PNAS.0709960105