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Magnesium in PDB 3h1g: Crystal Structure of Chey Mutant T84A of Helicobacter Pylori

Protein crystallography data

The structure of Crystal Structure of Chey Mutant T84A of Helicobacter Pylori, PDB code: 3h1g was solved by K.H.Lam, T.K.Ling, S.W.Au, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 17.39 / 1.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 70.409, 38.062, 39.020, 90.00, 107.58, 90.00
R / Rfree (%) 17.4 / 20.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Chey Mutant T84A of Helicobacter Pylori (pdb code 3h1g). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Chey Mutant T84A of Helicobacter Pylori, PDB code: 3h1g:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3h1g

Go back to Magnesium Binding Sites List in 3h1g
Magnesium binding site 1 out of 2 in the Crystal Structure of Chey Mutant T84A of Helicobacter Pylori


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 Chey Mutant T84A of Helicobacter Pylori within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg127

b:2.7
occ:1.00
O A:HOH304 3.2 8.0 1.0
O A:HOH300 3.3 15.1 1.0
CE A:MET12 3.5 8.7 1.0
CD A:LYS105 3.6 4.0 1.0
CB A:LYS105 3.8 4.4 1.0
CA A:PRO106 4.1 6.5 1.0
CG A:LYS105 4.1 4.7 1.0
CB A:PRO106 4.2 6.9 1.0
CE A:LYS105 4.6 5.8 1.0
N A:PRO106 4.7 6.2 1.0
CA A:LYS105 4.8 4.7 1.0
NZ A:LYS105 4.9 2.8 1.0

Magnesium binding site 2 out of 2 in 3h1g

Go back to Magnesium Binding Sites List in 3h1g
Magnesium binding site 2 out of 2 in the Crystal Structure of Chey Mutant T84A of Helicobacter Pylori


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Chey Mutant T84A of Helicobacter Pylori within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg128

b:7.5
occ:1.00
O A:ASN55 2.3 6.1 1.0
O3 A:SO4126 2.3 11.2 1.0
OD2 A:ASP53 2.4 4.8 1.0
O A:HOH143 2.4 4.2 1.0
OD1 A:ASP8 2.5 7.1 1.0
O A:HOH305 2.6 23.7 1.0
S A:SO4126 3.4 10.7 1.0
CG A:ASP8 3.4 6.9 1.0
C A:ASN55 3.4 6.2 1.0
CG A:ASP53 3.5 4.9 1.0
O4 A:SO4126 3.5 17.7 1.0
OD2 A:ASP8 3.8 6.1 1.0
O A:HOH187 3.9 19.5 1.0
CB A:ASP53 4.1 3.3 1.0
O2 A:SO4126 4.1 11.3 1.0
O A:HOH311 4.1 19.3 1.0
OD1 A:ASP7 4.2 8.1 1.0
CA A:ASN55 4.2 5.9 1.0
N A:ASN55 4.3 5.7 1.0
CB A:ASN55 4.3 6.0 1.0
OD1 A:ASP53 4.4 4.4 1.0
N A:MET56 4.5 6.5 1.0
N A:ASP8 4.5 5.7 1.0
CB A:MET56 4.5 6.6 1.0
O A:HOH309 4.5 24.7 1.0
O1 A:SO4126 4.6 16.4 1.0
NZ A:LYS105 4.6 2.8 1.0
CB A:ASP8 4.7 6.2 1.0
CA A:MET56 4.7 6.5 1.0
CG A:ASP7 4.8 5.3 1.0
OD2 A:ASP7 5.0 6.5 1.0

Reference:

K.H.Lam, T.K.Ling, S.W.Au. Crystal Structure of Activated CHEY1 From Helicobacter Pylori. J.Bacteriol. V. 192 2324 2010.
ISSN: ISSN 0021-9193
PubMed: 20207758
DOI: 10.1128/JB.00603-09
Page generated: Wed Aug 14 15:03:11 2024

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