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Manganese in PDB 1mih: A Role For Chey Glu 89 in Chez-Mediated Dephosphorylation of the E. Coli Chemotaxis Response Regulator Chey

Protein crystallography data

The structure of A Role For Chey Glu 89 in Chez-Mediated Dephosphorylation of the E. Coli Chemotaxis Response Regulator Chey, PDB code: 1mih was solved by R.E.Silversmith, G.P.Guanga, L.Betts, C.Chu, R.Zhao, R.B.Bourret, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.00 / 2.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.504, 53.615, 160.890, 90.00, 90.00, 90.00
R / Rfree (%) 22.6 / 27.7

Other elements in 1mih:

The structure of A Role For Chey Glu 89 in Chez-Mediated Dephosphorylation of the E. Coli Chemotaxis Response Regulator Chey also contains other interesting chemical elements:

Fluorine (F) 6 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the A Role For Chey Glu 89 in Chez-Mediated Dephosphorylation of the E. Coli Chemotaxis Response Regulator Chey (pdb code 1mih). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the A Role For Chey Glu 89 in Chez-Mediated Dephosphorylation of the E. Coli Chemotaxis Response Regulator Chey, PDB code: 1mih:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1mih

Go back to Manganese Binding Sites List in 1mih
Manganese binding site 1 out of 2 in the A Role For Chey Glu 89 in Chez-Mediated Dephosphorylation of the E. Coli Chemotaxis Response Regulator Chey


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of A Role For Chey Glu 89 in Chez-Mediated Dephosphorylation of the E. Coli Chemotaxis Response Regulator Chey within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn201

b:45.8
occ:1.00
F1 A:BEF130 2.1 30.4 1.0
OD1 A:ASP13 2.1 38.7 1.0
OD2 A:ASP57 2.3 26.5 1.0
O A:ARG59 2.4 34.8 1.0
O A:HOH405 2.5 22.0 1.0
CG A:ASP13 3.0 37.2 1.0
BE A:BEF130 3.2 31.3 1.0
OD2 A:ASP13 3.3 37.4 1.0
CG A:ASP57 3.3 28.2 1.0
C A:ARG59 3.6 35.2 1.0
OD1 A:ASP57 3.7 29.2 1.0
OD1 A:ASP12 3.8 32.2 1.0
CD2 A:PHE14 3.9 47.0 1.0
F3 A:BEF130 4.0 32.1 1.0
CE2 A:PHE14 4.2 48.5 1.0
CB A:ARG59 4.3 35.5 1.0
CA A:ARG59 4.3 35.7 1.0
F2 A:BEF130 4.4 33.0 1.0
N A:ASP13 4.4 37.5 1.0
CB A:ASP13 4.4 37.5 1.0
CG A:MET60 4.4 35.6 1.0
N A:ARG59 4.5 34.5 1.0
CB A:ASP57 4.6 27.8 1.0
CG A:ASP12 4.6 34.6 1.0
N A:MET60 4.7 36.1 1.0
NZ A:LYS109 4.8 30.5 1.0
CA A:MET60 4.9 36.8 1.0
CA A:ASP13 4.9 39.6 1.0
OD2 A:ASP12 5.0 35.7 1.0

Manganese binding site 2 out of 2 in 1mih

Go back to Manganese Binding Sites List in 1mih
Manganese binding site 2 out of 2 in the A Role For Chey Glu 89 in Chez-Mediated Dephosphorylation of the E. Coli Chemotaxis Response Regulator Chey


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of A Role For Chey Glu 89 in Chez-Mediated Dephosphorylation of the E. Coli Chemotaxis Response Regulator Chey within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn202

b:56.0
occ:1.00
F1 B:BEF131 1.8 30.4 1.0
OD1 B:ASP13 2.0 40.8 1.0
OD2 B:ASP57 2.3 29.1 1.0
O B:ARG59 2.4 40.0 1.0
O B:HOH404 2.4 22.7 1.0
CG B:ASP13 3.0 40.0 1.0
BE B:BEF131 3.2 28.6 1.0
OD2 B:ASP13 3.5 37.5 1.0
CG B:ASP57 3.5 32.2 1.0
C B:ARG59 3.6 37.9 1.0
OD1 B:ASP57 4.0 31.7 1.0
OD1 B:ASP12 4.0 35.6 1.0
F3 B:BEF131 4.1 28.3 1.0
CD2 B:PHE14 4.2 55.2 1.0
CB B:ARG59 4.2 37.6 1.0
F2 B:BEF131 4.3 28.8 1.0
CA B:ARG59 4.3 36.3 1.0
CB B:ASP13 4.4 40.9 1.0
N B:ASP13 4.4 39.2 1.0
CG B:MET60 4.5 32.1 1.0
N B:ARG59 4.5 34.3 1.0
CE2 B:PHE14 4.6 55.2 1.0
N B:MET60 4.6 38.9 1.0
CG B:ASP12 4.6 34.8 1.0
CB B:ASP57 4.7 30.2 1.0
NZ B:LYS109 4.8 33.4 1.0
OD2 B:ASP12 4.8 30.1 1.0
CA B:MET60 4.8 38.0 1.0
CA B:ASP13 4.8 41.3 1.0
O B:HOH425 5.0 40.2 1.0

Reference:

R.E.Silversmith, G.P.Guanga, L.Betts, C.Chu, R.Zhao, R.B.Bourret. Chez-Mediated Dephosphorylation of the Escherichia Coli Chemotaxis Response Regulator Chey: Role For Chey Glutamate 89. J.Bacteriol. V. 185 1495 2003.
ISSN: ISSN 0021-9193
PubMed: 12591865
DOI: 10.1128/JB.185.5.1495-1502.2003
Page generated: Sat Oct 5 11:43:07 2024

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