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Magnesium in PDB 3hzh: Crystal Structure of the Chex-Chey-BEF3-Mg+2 Complex From Borrelia Burgdorferi

Protein crystallography data

The structure of Crystal Structure of the Chex-Chey-BEF3-Mg+2 Complex From Borrelia Burgdorferi, PDB code: 3hzh was solved by Y.Pazy, R.E.Silversmith, M.Guarinari, R.Zhao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.64 / 1.96
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 63.705, 63.705, 175.685, 90.00, 90.00, 120.00
R / Rfree (%) 24.8 / 25.9

Other elements in 3hzh:

The structure of Crystal Structure of the Chex-Chey-BEF3-Mg+2 Complex From Borrelia Burgdorferi also contains other interesting chemical elements:

Fluorine (F) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Chex-Chey-BEF3-Mg+2 Complex From Borrelia Burgdorferi (pdb code 3hzh). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of the Chex-Chey-BEF3-Mg+2 Complex From Borrelia Burgdorferi, PDB code: 3hzh:

Magnesium binding site 1 out of 1 in 3hzh

Go back to Magnesium Binding Sites List in 3hzh
Magnesium binding site 1 out of 1 in the Crystal Structure of the Chex-Chey-BEF3-Mg+2 Complex From Borrelia Burgdorferi


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Chex-Chey-BEF3-Mg+2 Complex From Borrelia Burgdorferi within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg202

b:30.2
occ:1.00
OD1 A:ASP33 2.1 17.6 1.0
F1 A:BFD79 2.1 26.2 1.0
OD2 A:BFD79 2.2 27.9 1.0
O A:THR81 2.2 20.6 1.0
O A:HOH158 2.2 41.9 1.0
O A:HOH157 2.3 41.9 1.0
CG A:ASP33 3.0 21.3 1.0
CG A:BFD79 3.2 28.6 1.0
OD2 A:ASP33 3.3 21.4 1.0
BE A:BFD79 3.3 28.8 1.0
C A:THR81 3.4 24.2 1.0
OD1 A:BFD79 3.6 25.5 1.0
OD1 B:ASN99 3.9 22.1 1.0
CB A:THR81 4.0 23.2 1.0
O B:HOH164 4.0 36.4 1.0
CA A:THR81 4.1 21.7 1.0
OD1 A:ASP32 4.1 21.5 1.0
F3 A:BFD79 4.2 25.4 1.0
CG A:MET82 4.2 31.1 1.0
N A:THR81 4.3 22.9 1.0
F2 A:BFD79 4.3 26.0 1.0
CB A:ASP33 4.4 19.9 1.0
CG B:ASN99 4.4 24.4 1.0
N A:ASP33 4.4 23.2 1.0
N A:MET82 4.4 21.7 1.0
CB A:BFD79 4.5 25.2 1.0
CG2 A:THR81 4.6 19.8 1.0
O B:HOH192 4.6 41.7 1.0
ND2 B:ASN99 4.6 24.0 1.0
CA A:MET82 4.7 26.2 1.0
CG A:ASP32 4.7 21.1 1.0
OE1 B:GLU96 4.7 27.3 1.0
OD2 A:ASP32 4.7 19.0 1.0
CA A:ASP33 4.9 23.0 1.0
NZ A:LYS129 4.9 21.4 1.0
O B:HOH162 5.0 34.6 1.0

Reference:

Y.Pazy, M.A.Motaleb, M.T.Guarnieri, N.W.Charon, R.Zhao, R.E.Silversmith. Identical Phosphatase Mechanisms Achieved Through Distinct Modes of Binding Phosphoprotein Substrate. Proc.Natl.Acad.Sci.Usa V. 107 1924 2010.
ISSN: ISSN 0027-8424
PubMed: 20080618
DOI: 10.1073/PNAS.0911185107
Page generated: Mon Dec 14 08:15:15 2020

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