Magnesium in PDB 3klc: Crystal Structure of Hyperthermophilic Nitrilase

All present enzymatic activity of Crystal Structure of Hyperthermophilic Nitrilase:
3.5.1.6;

The structure of Crystal Structure of Hyperthermophilic Nitrilase, PDB code: 3klc was solved by J.Raczynska, C.Vorgias, G.Antranikian, W.Rypniewski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.69 / 1.76
Space group	P 41
Cell size a, b, c (Å), α, β, γ (°)	59.283, 59.283, 129.196, 90.00, 90.00, 90.00
R / Rfree (%)	15.5 / 19.2

The structure of Crystal Structure of Hyperthermophilic Nitrilase also contains other interesting chemical elements:

Bromine

(Br)

14 atoms

The binding sites of Magnesium atom in the Crystal Structure of Hyperthermophilic Nitrilase (pdb code 3klc). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Hyperthermophilic Nitrilase, PDB code: 3klc:

Magnesium binding site 1 out of 1 in the Crystal Structure of Hyperthermophilic Nitrilase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Hyperthermophilic Nitrilase within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg270 b:45.6 occ:1.00 O B:HOH359 2.0 38.1 1.0 O B:ARG255 2.0 28.2 1.0 O B:HOH340 2.1 45.6 1.0 O B:HOH286 2.1 33.3 1.0 O B:HOH296 2.1 31.2 1.0 OE2 B:GLU257 2.3 28.6 1.0 C B:ARG255 3.2 27.0 1.0 CD B:GLU257 3.4 30.9 1.0 OE1 B:GLU257 3.7 31.8 1.0 O B:LYS253 3.8 28.5 1.0 CA B:ARG256 4.0 28.9 1.0 N B:ARG256 4.0 27.4 1.0 CA B:ARG255 4.2 26.0 1.0 O B:HOH360 4.2 34.5 1.0 N B:GLU257 4.3 28.6 1.0 N B:ARG255 4.3 25.0 1.0 CB B:ARG255 4.6 25.1 1.0 O B:PHE252 4.7 25.1 1.0 O A:HOH319 4.7 32.4 1.0 CG B:GLU257 4.7 29.2 1.0 C B:ARG256 4.7 29.0 1.0 CG B:ARG256 4.8 32.4 1.0 C B:LYS253 4.8 26.8 1.0 C B:ASP254 4.8 25.6 1.0

J.E.Raczynska, C.E.Vorgias, G.Antranikian, W.Rypniewski. Crystallographic Analysis of A Thermoactive Nitrilase. J.Struct.Biol. V. 173 294 2010.
ISSN: ISSN 1047-8477
PubMed: 21095228
DOI: 10.1016/J.JSB.2010.11.017