Manganese in PDB 3ffx: Crystal Structure of Chey Triple Mutant F14E, N59R, E89H Complexed with BEF3- and MN2+

The structure of Crystal Structure of Chey Triple Mutant F14E, N59R, E89H Complexed with BEF3- and MN2+, PDB code: 3ffx was solved by Y.Pazy, E.J.Collins, R.B.Bourret, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.97 / 2.01
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	53.564, 53.408, 161.839, 90.00, 90.00, 90.00
R / Rfree (%)	17.8 / 21

The structure of Crystal Structure of Chey Triple Mutant F14E, N59R, E89H Complexed with BEF3- and MN2+ also contains other interesting chemical elements:

Fluorine

(F)

6 atoms

The binding sites of Manganese atom in the Crystal Structure of Chey Triple Mutant F14E, N59R, E89H Complexed with BEF3- and MN2+ (pdb code 3ffx). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Chey Triple Mutant F14E, N59R, E89H Complexed with BEF3- and MN2+, PDB code: 3ffx:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of Chey Triple Mutant F14E, N59R, E89H Complexed with BEF3- and MN2+


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Chey Triple Mutant F14E, N59R, E89H Complexed with BEF3- and MN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn202 b:26.0 occ:1.00 F1 A:BEF130 2.0 26.1 1.0 O A:HOH318 2.0 22.5 1.0 OD2 A:ASP57 2.2 22.3 1.0 OD1 A:ASP13 2.2 20.3 1.0 O A:ARG59 2.3 22.2 1.0 O A:HOH223 2.3 20.0 1.0 CG A:ASP57 3.1 19.5 1.0 CG A:ASP13 3.2 23.1 1.0 BE A:BEF130 3.2 23.0 1.0 OD1 A:ASP57 3.4 18.9 1.0 C A:ARG59 3.4 22.8 1.0 OD2 A:ASP13 3.5 28.4 1.0 OD1 A:ASP12 4.0 19.5 1.0 CB A:ARG59 4.1 23.4 0.5 CA A:ARG59 4.1 22.9 0.5 CA A:ARG59 4.1 22.9 0.5 CB A:ARG59 4.2 23.2 0.5 OE1 A:GLU14 4.3 27.3 1.0 N A:ARG59 4.3 22.7 1.0 F3 A:BEF130 4.3 21.2 1.0 CG A:MET60 4.3 20.7 1.0 O A:HOH343 4.4 51.5 1.0 O A:HOH254 4.4 43.6 1.0 CB A:ASP57 4.5 19.7 1.0 N A:ASP13 4.5 20.3 1.0 N A:MET60 4.5 22.0 1.0 F2 A:BEF130 4.5 23.5 1.0 CB A:ASP13 4.5 21.1 1.0 NZ A:LYS109 4.6 18.1 1.0 O A:HOH216 4.6 33.2 1.0 CG A:ARG59 4.6 24.7 0.5 CG A:ASP12 4.7 20.3 1.0 CA A:MET60 4.8 21.8 1.0 OD2 A:ASP12 4.8 19.8 1.0 CG A:GLU14 4.8 24.9 1.0 CA A:ASP13 5.0 21.2 1.0 O A:HOH174 5.0 47.8 1.0 CD A:GLU14 5.0 26.2 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of Chey Triple Mutant F14E, N59R, E89H Complexed with BEF3- and MN2+


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Chey Triple Mutant F14E, N59R, E89H Complexed with BEF3- and MN2+ within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn202 b:30.0 occ:1.00 F1 B:BEF130 2.0 27.2 1.0 O B:HOH319 2.1 28.8 1.0 OD2 B:ASP57 2.2 22.1 1.0 OD1 B:ASP13 2.2 29.9 1.0 O B:ARG59 2.3 24.8 1.0 O B:HOH199 2.3 22.9 1.0 CG B:ASP57 3.2 22.0 1.0 BE B:BEF130 3.2 24.8 1.0 CG B:ASP13 3.2 26.8 1.0 C B:ARG59 3.4 24.7 1.0 OD1 B:ASP57 3.5 22.3 1.0 OD2 B:ASP13 3.5 33.9 1.0 OD1 B:ASP12 4.0 20.8 1.0 O B:HOH331 4.1 42.6 1.0 CA B:ARG59 4.2 24.4 0.5 CA B:ARG59 4.2 24.9 0.5 CB B:ARG59 4.2 24.4 0.5 CB B:ARG59 4.2 24.8 0.5 CG B:MET60 4.3 24.1 1.0 N B:ARG59 4.3 24.2 1.0 F3 B:BEF130 4.4 23.3 1.0 O B:HOH203 4.4 45.5 1.0 OE1 B:GLU14 4.5 31.2 1.0 F2 B:BEF130 4.5 26.9 1.0 N B:MET60 4.5 24.6 1.0 CB B:ASP57 4.5 21.2 1.0 O B:HOH332 4.5 42.6 1.0 CB B:ASP13 4.6 24.6 1.0 CG B:ARG59 4.6 25.5 0.5 N B:ASP13 4.6 23.4 1.0 NZ B:LYS109 4.7 23.3 1.0 CG B:ASP12 4.7 22.1 1.0 CA B:MET60 4.7 24.2 1.0 OD2 B:ASP12 4.9 22.4 1.0 CG B:GLU14 4.9 28.5 1.0

Y.Pazy, A.C.Wollish, S.A.Thomas, P.J.Miller, E.J.Collins, R.B.Bourret, R.E.Silversmith. Matching Biochemical Reaction Kinetics to the Timescales of Life: Structural Determinants That Influence the Autodephosphorylation Rate of Response Regulator Proteins. J.Mol.Biol. V. 392 1205 2009.
ISSN: ISSN 0022-2836
PubMed: 19646451
DOI: 10.1016/J.JMB.2009.07.064