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Magnesium in PDB 4zms: Structure of the Full-Length Response Regulator SPR1814 in Complex with A Phosphate Analogue and B3C

Protein crystallography data

The structure of Structure of the Full-Length Response Regulator SPR1814 in Complex with A Phosphate Analogue and B3C, PDB code: 4zms 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) 37.82 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 40.980, 115.526, 50.073, 90.00, 92.41, 90.00
R / Rfree (%) 16.5 / 21.5

Other elements in 4zms:

The structure of Structure of the Full-Length Response Regulator SPR1814 in Complex with A Phosphate Analogue and B3C also contains other interesting chemical elements:

Fluorine (F) 6 atoms
Bromine (Br) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the Full-Length Response Regulator SPR1814 in Complex with A Phosphate Analogue and B3C (pdb code 4zms). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of the Full-Length Response Regulator SPR1814 in Complex with A Phosphate Analogue and B3C, PDB code: 4zms:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 4zms

Go back to Magnesium Binding Sites List in 4zms
Magnesium binding site 1 out of 2 in the Structure of the Full-Length Response Regulator SPR1814 in Complex with A Phosphate Analogue and B3C


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Full-Length Response Regulator SPR1814 in Complex with A Phosphate Analogue and B3C within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg201

b:12.1
occ:1.00
F1 A:BEF202 1.9 10.3 1.0
O A:HOH433 1.9 12.0 1.0
O A:GLU55 2.1 11.5 1.0
OD1 A:ASP8 2.1 11.9 1.0
O A:HOH366 2.1 11.7 1.0
OD2 A:ASP53 2.2 8.6 1.0
CG A:ASP53 3.1 10.4 1.0
CG A:ASP8 3.1 16.9 1.0
C A:GLU55 3.2 13.1 1.0
OD1 A:ASP53 3.3 9.8 1.0
HB2 A:GLU55 3.4 15.1 1.0
OD2 A:ASP8 3.4 13.3 1.0
BE A:BEF202 3.4 20.8 1.0
H A:ASP8 3.7 12.6 1.0
HG2 A:MET56 3.8 12.2 1.0
O A:HOH460 3.9 17.5 1.0
CB A:GLU55 4.0 12.6 1.0
CA A:GLU55 4.0 11.7 1.0
OE1 A:GLU7 4.0 10.0 1.0
H A:GLU55 4.0 13.6 1.0
HG3 A:MET56 4.1 12.2 1.0
HB3 A:GLU55 4.1 15.1 1.0
HA A:MET56 4.1 14.4 1.0
O A:HOH383 4.1 27.2 1.0
F3 A:BEF202 4.1 9.8 1.0
F2 A:BEF202 4.2 13.1 1.0
N A:GLU55 4.2 11.3 1.0
HZ1 A:LYS103 4.2 16.9 1.0
N A:MET56 4.3 16.3 1.0
O A:HOH486 4.3 37.2 1.0
HZ2 A:LYS103 4.3 16.9 1.0
O A:HOH320 4.4 17.3 1.0
CG A:MET56 4.4 10.2 1.0
H A:GLN9 4.4 16.6 1.0
CB A:ASP8 4.4 12.4 1.0
CB A:ASP53 4.4 9.2 1.0
HB3 A:ASP53 4.5 11.1 1.0
N A:ASP8 4.5 10.5 1.0
HE2 A:PHE83 4.5 22.1 1.0
OE2 A:GLU7 4.6 10.4 1.0
CA A:MET56 4.7 12.0 1.0
NZ A:LYS103 4.7 14.1 1.0
CD A:GLU7 4.7 13.3 1.0
HB3 A:ASP8 4.7 14.9 1.0
HB2 A:ASP53 4.8 11.1 1.0
HZ3 A:LYS103 4.8 16.9 1.0
HA A:GLU55 4.9 14.1 1.0
CA A:ASP8 4.9 12.2 1.0
N A:GLN9 5.0 13.8 1.0

Magnesium binding site 2 out of 2 in 4zms

Go back to Magnesium Binding Sites List in 4zms
Magnesium binding site 2 out of 2 in the Structure of the Full-Length Response Regulator SPR1814 in Complex with A Phosphate Analogue and B3C


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the Full-Length Response Regulator SPR1814 in Complex with A Phosphate Analogue and B3C within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg201

b:13.2
occ:1.00
F2 B:BEF202 2.0 12.8 1.0
OD1 B:ASP53 2.0 9.8 1.0
O B:GLU55 2.1 15.4 1.0
OD1 B:ASP8 2.1 15.6 1.0
O B:HOH394 2.1 13.2 1.0
O B:HOH451 2.2 15.9 1.0
CG B:ASP53 3.0 14.2 1.0
CG B:ASP8 3.0 15.6 1.0
C B:GLU55 3.2 15.2 1.0
OD2 B:ASP8 3.3 22.2 1.0
OD2 B:ASP53 3.4 10.8 1.0
BE B:BEF202 3.5 16.1 1.0
H B:ASP8 3.5 17.6 1.0
HB2 B:GLU55 3.6 17.9 1.0
HG2 B:MET56 3.6 20.6 1.0
OE1 B:GLU7 3.9 11.1 1.0
HA B:MET56 4.0 20.5 1.0
O B:HOH478 4.0 19.4 1.0
CA B:GLU55 4.1 13.7 1.0
CB B:GLU55 4.1 14.9 1.0
H B:GLU55 4.2 19.1 1.0
HZ1 B:LYS103 4.2 12.8 1.0
HB3 B:GLU55 4.2 17.9 1.0
F1 B:BEF202 4.3 10.5 1.0
N B:MET56 4.3 13.0 1.0
H B:GLN9 4.3 15.1 1.0
HG3 B:MET56 4.3 20.6 1.0
F3 B:BEF202 4.3 13.9 1.0
CB B:ASP53 4.3 10.6 1.0
HB3 B:ASP53 4.3 12.7 1.0
CB B:ASP8 4.3 13.3 1.0
N B:GLU55 4.3 15.9 1.0
N B:ASP8 4.4 14.7 1.0
CG B:MET56 4.4 17.2 1.0
O B:HOH506 4.4 21.6 1.0
HZ2 B:LYS103 4.5 12.8 1.0
O B:HOH311 4.5 19.4 1.0
HB3 B:ASP8 4.5 16.0 1.0
CA B:MET56 4.5 17.1 1.0
HE2 B:PHE83 4.5 29.9 1.0
CD B:GLU7 4.6 11.3 1.0
NZ B:LYS103 4.7 10.7 1.0
OE2 B:GLU7 4.7 8.9 1.0
HB2 B:ASP53 4.7 12.7 1.0
HZ3 B:LYS103 4.7 12.8 1.0
O B:HOH453 4.8 41.8 1.0
CA B:ASP8 4.8 14.0 1.0
N B:GLN9 4.9 12.6 1.0
HA B:GLU7 4.9 15.7 1.0
HA B:GLU55 5.0 16.4 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 19:57:39 2020

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