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Manganese in PDB 3fgz: Crystal Structure of Chey Triple Mutant F14E, N59M, E89R Complexed with BEF3- and MN2+

Protein crystallography data

The structure of Crystal Structure of Chey Triple Mutant F14E, N59M, E89R Complexed with BEF3- and MN2+, PDB code: 3fgz was solved by A.C.Wollish, P.J.Miller, 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) 80.85 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.534, 53.485, 161.853, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 22

Other elements in 3fgz:

The structure of Crystal Structure of Chey Triple Mutant F14E, N59M, E89R Complexed with BEF3- and MN2+ also contains other interesting chemical elements:

Fluorine (F) 6 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Chey Triple Mutant F14E, N59M, E89R Complexed with BEF3- and MN2+ (pdb code 3fgz). 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, N59M, E89R Complexed with BEF3- and MN2+, PDB code: 3fgz:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 3fgz

Go back to Manganese Binding Sites List in 3fgz
Manganese binding site 1 out of 2 in the Crystal Structure of Chey Triple Mutant F14E, N59M, E89R 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, N59M, E89R Complexed with BEF3- and MN2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn202

b:23.2
occ:1.00
F1 A:BEF130 2.0 24.8 1.0
OD2 A:ASP57 2.1 20.2 1.0
OD1 A:ASP13 2.1 21.9 1.0
O A:HOH151 2.2 22.5 1.0
O A:HOH192 2.2 19.5 1.0
O A:MET59 2.3 20.7 1.0
CG A:ASP57 3.1 18.4 1.0
CG A:ASP13 3.1 22.1 1.0
BE A:BEF130 3.2 23.1 1.0
OD1 A:ASP57 3.4 19.8 1.0
OD2 A:ASP13 3.4 26.1 1.0
C A:MET59 3.4 21.6 1.0
OD1 A:ASP12 3.9 18.4 1.0
CA A:MET59 4.1 22.5 1.0
CB A:MET59 4.2 22.8 1.0
N A:MET59 4.2 20.7 1.0
OE1 A:GLU14 4.3 29.3 1.0
CG A:MET60 4.3 20.2 1.0
F3 A:BEF130 4.3 22.5 1.0
O A:HOH156 4.4 29.6 1.0
CB A:ASP57 4.4 18.4 1.0
N A:ASP13 4.5 19.4 1.0
CB A:ASP13 4.5 20.5 1.0
N A:MET60 4.5 21.0 1.0
F2 A:BEF130 4.5 22.4 1.0
NZ A:LYS109 4.5 19.5 1.0
CG A:ASP12 4.6 18.9 1.0
CG A:GLU14 4.7 25.6 1.0
OD2 A:ASP12 4.7 17.6 1.0
CA A:MET60 4.8 20.6 1.0
CA A:ASP13 5.0 20.6 1.0
CD A:GLU14 5.0 30.2 1.0

Manganese binding site 2 out of 2 in 3fgz

Go back to Manganese Binding Sites List in 3fgz
Manganese binding site 2 out of 2 in the Crystal Structure of Chey Triple Mutant F14E, N59M, E89R 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, N59M, E89R Complexed with BEF3- and MN2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn202

b:25.4
occ:1.00
F2 B:BEF130 2.0 26.8 1.0
OD2 B:ASP57 2.1 18.9 1.0
OD1 B:ASP13 2.2 25.1 1.0
O B:HOH178 2.2 26.7 1.0
O B:MET59 2.2 22.3 1.0
O B:HOH147 2.3 20.9 1.0
CG B:ASP57 3.1 20.5 1.0
CG B:ASP13 3.1 24.4 1.0
BE B:BEF130 3.2 26.2 1.0
C B:MET59 3.4 23.1 1.0
OD2 B:ASP13 3.4 27.5 1.0
OD1 B:ASP57 3.4 17.9 1.0
OD1 B:ASP12 3.9 20.5 1.0
CA B:MET59 4.1 23.6 1.0
CB B:MET59 4.2 22.8 1.0
CG B:MET60 4.3 19.7 1.0
O B:HOH205 4.3 40.0 1.0
N B:MET59 4.3 21.8 1.0
OE1 B:GLU14 4.3 29.3 1.0
F1 B:BEF130 4.4 23.9 1.0
CB B:ASP57 4.4 19.8 1.0
N B:MET60 4.5 22.0 1.0
CB B:ASP13 4.5 21.8 1.0
N B:ASP13 4.5 21.1 1.0
F3 B:BEF130 4.5 25.7 1.0
NZ B:LYS109 4.6 21.6 1.0
CG B:ASP12 4.6 21.2 1.0
CA B:MET60 4.7 21.4 1.0
OD2 B:ASP12 4.8 21.5 1.0
CG B:GLU14 4.9 26.8 1.0
CA B:ASP13 5.0 21.9 1.0

Reference:

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
Page generated: Tue Dec 15 04:09:30 2020

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