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Magnesium in PDB 6s2j: Square Conformation of Ktra R16K Mutant Ring with Bound Atp

Protein crystallography data

The structure of Square Conformation of Ktra R16K Mutant Ring with Bound Atp, PDB code: 6s2j was solved by C.M.Teixeira-Duarte, F.Fonseca, J.H.Morais-Cabral, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.17 / 2.67
Space group I 4
Cell size a, b, c (Å), α, β, γ (°) 123.276, 123.276, 84.451, 90.00, 90.00, 90.00
R / Rfree (%) 19 / 23.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Square Conformation of Ktra R16K Mutant Ring with Bound Atp (pdb code 6s2j). 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 Square Conformation of Ktra R16K Mutant Ring with Bound Atp, PDB code: 6s2j:

Magnesium binding site 1 out of 1 in 6s2j

Go back to Magnesium Binding Sites List in 6s2j
Magnesium binding site 1 out of 1 in the Square Conformation of Ktra R16K Mutant Ring with Bound Atp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Square Conformation of Ktra R16K Mutant Ring with Bound Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg603

b:74.3
occ:1.00
O A:HOH702 2.1 68.4 1.0
O A:HOH701 2.1 66.7 1.0
OE2 A:GLU125 2.2 84.9 1.0
OE2 B:GLU125 2.3 92.7 1.0
O2G A:ATP602 2.5 90.2 1.0
O2G A:ATP601 2.5 54.6 1.0
HG2 B:GLU125 3.0 84.1 1.0
HZ1 A:LYS103 3.2 0.6 1.0
CD B:GLU125 3.2 98.4 1.0
HG2 A:GLU125 3.3 79.0 1.0
CD A:GLU125 3.3 96.2 1.0
HZ1 B:LYS103 3.4 0.9 1.0
CG B:GLU125 3.5 70.1 1.0
HG3 B:GLU125 3.6 84.1 1.0
CG A:GLU125 3.7 65.8 1.0
HZ1 B:LYS16 3.7 0.8 1.0
HE2 A:LYS16 3.8 92.2 1.0
HZ3 A:LYS16 3.8 0.5 1.0
HE2 B:LYS16 3.8 88.4 1.0
HG3 A:GLU125 3.8 79.0 1.0
HZ3 A:LYS103 3.9 0.6 1.0
NZ A:LYS103 3.9 93.8 1.0
O1B A:ATP601 4.0 74.5 1.0
PG A:ATP602 4.0 75.7 1.0
PG A:ATP601 4.0 81.3 1.0
NZ B:LYS103 4.2 98.3 1.0
HZ3 B:LYS103 4.2 0.9 1.0
HE3 B:LYS16 4.2 88.4 1.0
HE3 A:LYS16 4.3 92.2 1.0
CE B:LYS16 4.3 73.7 1.0
CE A:LYS16 4.4 76.8 1.0
OE1 B:GLU125 4.4 88.6 1.0
NZ B:LYS16 4.4 97.3 1.0
OE1 A:GLU125 4.4 93.7 1.0
NZ A:LYS16 4.4 91.3 1.0
HZ2 A:LYS103 4.4 0.6 1.0
O1B A:ATP602 4.5 0.3 1.0
O2B A:ATP601 4.5 93.8 1.0
O3B A:ATP602 4.6 68.0 1.0
PB A:ATP601 4.6 86.1 1.0
HZ2 B:LYS103 4.6 0.9 1.0
HE2 A:LYS103 4.6 0.4 1.0
O3B A:ATP601 4.7 87.1 1.0
O1G A:ATP601 4.7 73.6 1.0
HZ2 A:LYS16 4.7 0.5 1.0
HZ3 B:LYS16 4.7 0.8 1.0
O1G A:ATP602 4.8 83.8 1.0
O2B A:ATP602 4.8 89.2 1.0
PB A:ATP602 4.8 74.1 1.0
CE A:LYS103 4.9 86.2 1.0
O3G A:ATP602 4.9 51.9 1.0
CB B:GLU125 4.9 73.7 1.0
O3G A:ATP601 5.0 95.7 1.0
HE22 A:GLN105 5.0 1.0 1.0

Reference:

C.M.Teixeira-Duarte, F.Fonseca, J.H.Morais Cabral. Activation of A Nucleotide-Dependent Rck Domain Requires Binding of A Cation Cofactor to A Conserved Site. Elife V. 8 2019.
ISSN: ESSN 2050-084X
PubMed: 31868587
DOI: 10.7554/ELIFE.50661
Page generated: Tue Oct 1 17:36:37 2024

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