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Magnesium in PDB 5hg2: Backbone Modifications in the Protein GB1 Helix: Beta-3-ALA24, Beta-3- LYS28, Beta-3-LYS31, Beta-2-ASN35

Protein crystallography data

The structure of Backbone Modifications in the Protein GB1 Helix: Beta-3-ALA24, Beta-3- LYS28, Beta-3-LYS31, Beta-2-ASN35, PDB code: 5hg2 was solved by N.A.Tavenor, Z.E.Reinert, G.A.Lengyel, B.D.Griffith, W.S.Horne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 51.95 / 1.80
Space group P 41
Cell size a, b, c (Å), α, β, γ (°) 51.947, 51.947, 96.404, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 21.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Backbone Modifications in the Protein GB1 Helix: Beta-3-ALA24, Beta-3- LYS28, Beta-3-LYS31, Beta-2-ASN35 (pdb code 5hg2). 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 Backbone Modifications in the Protein GB1 Helix: Beta-3-ALA24, Beta-3- LYS28, Beta-3-LYS31, Beta-2-ASN35, PDB code: 5hg2:

Magnesium binding site 1 out of 1 in 5hg2

Go back to Magnesium Binding Sites List in 5hg2
Magnesium binding site 1 out of 1 in the Backbone Modifications in the Protein GB1 Helix: Beta-3-ALA24, Beta-3- LYS28, Beta-3-LYS31, Beta-2-ASN35


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Backbone Modifications in the Protein GB1 Helix: Beta-3-ALA24, Beta-3- LYS28, Beta-3-LYS31, Beta-2-ASN35 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg103

b:35.9
occ:1.00
O A:HOH258 2.0 35.5 1.0
O D:HOH259 2.2 34.2 1.0
O D:HOH216 2.2 25.4 1.0
O D:HOH204 2.5 27.4 1.0
O D:HOH261 2.6 33.0 1.0
O A:HOH237 4.0 31.4 1.0
O D:HOH228 4.4 19.1 1.0
O A:HOH270 4.4 47.3 1.0
OD2 D:ASP36 4.4 20.3 1.0
OD1 D:ASP36 4.4 24.6 1.0
O D:HOH221 4.6 18.3 1.0
O3 A:GOL101 4.7 19.1 1.0
CD D:GLN32 4.8 18.7 1.0
CG D:ASP36 4.9 22.6 1.0
CG D:GLN32 5.0 19.8 1.0

Reference:

N.A.Tavenor, Z.E.Reinert, G.A.Lengyel, B.D.Griffith, W.S.Horne. Comparison of Design Strategies For Alpha-Helix Backbone Modification in A Protein Tertiary Fold. Chem.Commun.(Camb.) V. 52 3789 2016.
ISSN: ESSN 1364-548X
PubMed: 26853882
DOI: 10.1039/C6CC00273K
Page generated: Sun Sep 29 15:49:35 2024

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