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Magnesium in PDB 4zmr: Structural Characterization of the Full-Length Response Regulator SPR1814 in Complex with A Phosphate Analogue Reveals A Novel Conformational Plasticity of the Linker Region

Protein crystallography data

The structure of Structural Characterization of the Full-Length Response Regulator SPR1814 in Complex with A Phosphate Analogue Reveals A Novel Conformational Plasticity of the Linker Region, PDB code: 4zmr was solved by Y.M.Chi, A.Park, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.71 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 40.233, 114.491, 50.148, 90.00, 92.12, 90.00
R / Rfree (%) 18 / 22.7

Other elements in 4zmr:

The structure of Structural Characterization of the Full-Length Response Regulator SPR1814 in Complex with A Phosphate Analogue Reveals A Novel Conformational Plasticity of the Linker Region also contains other interesting chemical elements:

Fluorine (F) 6 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structural Characterization of the Full-Length Response Regulator SPR1814 in Complex with A Phosphate Analogue Reveals A Novel Conformational Plasticity of the Linker Region (pdb code 4zmr). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structural Characterization of the Full-Length Response Regulator SPR1814 in Complex with A Phosphate Analogue Reveals A Novel Conformational Plasticity of the Linker Region, PDB code: 4zmr:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 4zmr

Go back to Magnesium Binding Sites List in 4zmr
Magnesium binding site 1 out of 2 in the Structural Characterization of the Full-Length Response Regulator SPR1814 in Complex with A Phosphate Analogue Reveals A Novel Conformational Plasticity of the Linker Region


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structural Characterization of the Full-Length Response Regulator SPR1814 in Complex with A Phosphate Analogue Reveals A Novel Conformational Plasticity of the Linker Region within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg201

b:17.9
occ:1.00
O A:GLU55 1.9 13.8 1.0
F1 A:BEF202 2.0 16.4 1.0
OD1 A:ASP8 2.0 18.2 1.0
OD2 A:ASP53 2.2 19.3 1.0
O A:HOH393 2.2 21.2 1.0
O A:HOH322 2.4 18.9 1.0
CG A:ASP8 2.9 18.0 1.0
C A:GLU55 3.1 18.3 1.0
CG A:ASP53 3.2 18.8 1.0
OD2 A:ASP8 3.2 19.4 1.0
BE A:BEF202 3.4 26.6 1.0
OD1 A:ASP53 3.5 13.6 1.0
HB2 A:GLU55 3.6 31.2 1.0
HG2 A:MET56 3.7 20.5 1.0
H A:ASP8 3.7 18.0 1.0
H A:GLU55 3.9 18.2 1.0
HA A:MET56 3.9 22.1 1.0
CA A:GLU55 3.9 20.5 1.0
HB3 A:GLU55 4.0 31.2 1.0
CB A:GLU55 4.0 26.0 1.0
O A:HOH409 4.0 17.8 1.0
OE1 A:GLU7 4.1 16.2 1.0
HG3 A:MET56 4.1 20.5 1.0
N A:GLU55 4.1 15.2 1.0
N A:MET56 4.2 14.2 1.0
F3 A:BEF202 4.2 21.3 1.0
CB A:ASP8 4.3 19.3 1.0
F2 A:BEF202 4.3 31.5 1.0
CG A:MET56 4.3 17.1 1.0
O A:HOH302 4.5 28.6 1.0
CB A:ASP53 4.5 15.3 1.0
HB3 A:ASP8 4.5 23.2 1.0
CA A:MET56 4.5 18.4 1.0
HB3 A:ASP53 4.5 18.3 1.0
N A:ASP8 4.5 15.0 1.0
H A:GLN9 4.5 20.6 1.0
HZ2 A:LYS103 4.5 32.4 1.0
HZ1 A:LYS103 4.5 32.4 1.0
O A:HOH416 4.7 35.6 1.0
CD A:GLU7 4.7 20.4 1.0
OE2 A:GLU7 4.8 13.2 1.0
HA A:GLU55 4.8 24.6 1.0
O A:HOH429 4.8 49.8 1.0
HB2 A:ASP53 4.9 18.3 1.0
CA A:ASP8 4.9 19.5 1.0
H A:MET56 4.9 17.0 1.0
NZ A:LYS103 4.9 27.0 1.0
HB2 A:ASP8 5.0 23.2 1.0
HE2 A:PHE83 5.0 34.7 1.0
CB A:MET56 5.0 20.9 1.0

Magnesium binding site 2 out of 2 in 4zmr

Go back to Magnesium Binding Sites List in 4zmr
Magnesium binding site 2 out of 2 in the Structural Characterization of the Full-Length Response Regulator SPR1814 in Complex with A Phosphate Analogue Reveals A Novel Conformational Plasticity of the Linker Region


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structural Characterization of the Full-Length Response Regulator SPR1814 in Complex with A Phosphate Analogue Reveals A Novel Conformational Plasticity of the Linker Region within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg201

b:18.2
occ:1.00
F2 B:BEF202 1.9 17.7 1.0
OD1 B:ASP8 2.0 15.9 1.0
OD1 B:ASP53 2.0 16.9 1.0
O B:GLU55 2.1 14.2 1.0
O B:HOH389 2.1 18.4 1.0
O B:HOH325 2.1 13.8 1.0
CG B:ASP8 3.0 21.0 1.0
CG B:ASP53 3.0 20.8 1.0
OD2 B:ASP8 3.2 20.1 1.0
C B:GLU55 3.3 16.5 1.0
OD2 B:ASP53 3.3 11.7 1.0
BE B:BEF202 3.5 24.8 1.0
HB2 B:GLU55 3.5 19.8 1.0
H B:ASP8 3.6 21.2 1.0
HG2 B:MET56 3.6 25.4 1.0
O B:HOH413 3.9 29.7 1.0
H B:GLU55 3.9 20.6 1.0
HA B:MET56 4.0 23.4 1.0
OE1 B:GLU7 4.0 12.8 1.0
CA B:GLU55 4.1 13.8 1.0
N B:GLU55 4.2 17.1 1.0
F3 B:BEF202 4.2 27.8 1.0
CB B:GLU55 4.2 16.5 1.0
HG3 B:MET56 4.2 25.4 1.0
F1 B:BEF202 4.2 24.1 1.0
HZ1 B:LYS103 4.3 22.8 1.0
N B:MET56 4.3 17.6 1.0
CB B:ASP53 4.3 18.3 1.0
CG B:MET56 4.3 21.1 1.0
CB B:ASP8 4.4 21.3 1.0
O B:HOH309 4.4 27.4 1.0
HB3 B:ASP53 4.4 22.0 1.0
N B:ASP8 4.4 17.7 1.0
HB3 B:GLU55 4.5 19.8 1.0
HZ2 B:LYS103 4.5 22.8 1.0
HE2 B:PHE83 4.6 43.8 1.0
CA B:MET56 4.6 19.5 1.0
H B:GLN9 4.6 17.7 1.0
HB3 B:ASP8 4.6 25.6 1.0
O B:HOH408 4.6 29.6 1.0
OE2 B:GLU7 4.7 16.5 1.0
CD B:GLU7 4.7 14.6 1.0
HB2 B:ASP53 4.7 22.0 1.0
NZ B:LYS103 4.8 19.0 1.0
CA B:ASP8 4.9 20.3 1.0
HA B:GLU7 4.9 19.2 1.0
HZ3 B:LYS103 4.9 22.8 1.0
HA B:GLU55 5.0 16.6 1.0

Reference:

A.K.Park, J.H.Lee, Y.M.Chi, H.Park. Structural Characterization of the Full-Length Response Regulator SPR1814 in Complex with A Phosphate Analogue Reveals A Novel Conformational Plasticity of the Linker Region Biochem.Biophys.Res.Commun. V. 473 625 2016.
ISSN: ESSN 1090-2104
PubMed: 27038544
DOI: 10.1016/J.BBRC.2016.03.144
Page generated: Mon Dec 14 19:57:38 2020

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