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Magnesium in PDB 5nro: Structure of Full-Length Dnak with Bound J-Domain

Protein crystallography data

The structure of Structure of Full-Length Dnak with Bound J-Domain, PDB code: 5nro was solved by J.Kopp, R.Kityk, M.P.Mayer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.12 / 3.25
Space group P 62 2 2
Cell size a, b, c (Å), α, β, γ (°) 127.246, 127.246, 252.885, 90.00, 90.00, 120.00
R / Rfree (%) 21.6 / 23.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Full-Length Dnak with Bound J-Domain (pdb code 5nro). 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 Structure of Full-Length Dnak with Bound J-Domain, PDB code: 5nro:

Magnesium binding site 1 out of 1 in 5nro

Go back to Magnesium Binding Sites List in 5nro
Magnesium binding site 1 out of 1 in the Structure of Full-Length Dnak with Bound J-Domain


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Full-Length Dnak with Bound J-Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg701

b:48.1
occ:1.00
O A:HOH802 1.7 53.6 1.0
O A:HOH803 2.0 55.4 1.0
O A:HOH804 2.0 68.6 1.0
O2B A:ATP700 2.1 78.2 1.0
O A:HOH801 2.2 42.5 1.0
O1G A:ATP700 2.3 71.0 1.0
PB A:ATP700 3.6 90.9 1.0
OE1 A:GLU171 3.6 0.1 1.0
PG A:ATP700 3.7 76.4 1.0
OE2 A:GLU171 3.7 86.7 1.0
CD A:GLU171 3.7 94.4 1.0
OD1 A:ASP8 3.8 0.7 1.0
OD2 A:ASP8 4.0 87.8 1.0
O3B A:ATP700 4.1 71.9 1.0
O2A A:ATP700 4.3 66.3 1.0
CG A:ASP8 4.3 88.9 1.0
O2G A:ATP700 4.4 69.3 1.0
OD2 A:ASP194 4.4 0.9 1.0
OD1 A:ASP194 4.4 94.9 1.0
O3A A:ATP700 4.5 63.7 1.0
CG2 A:VAL371 4.6 92.5 1.0
O1B A:ATP700 4.7 63.2 1.0
CG A:GLU171 4.7 81.2 1.0
O3G A:ATP700 4.8 69.0 1.0
CG A:ASP194 4.9 96.9 1.0
PA A:ATP700 4.9 58.3 1.0

Reference:

R.Kityk, J.Kopp, M.P.Mayer. Molecular Mechanism of J-Domain-Triggered Atp Hydrolysis By HSP70 Chaperones. Mol. Cell V. 69 227 2018.
ISSN: ISSN 1097-4164
PubMed: 29290615
DOI: 10.1016/J.MOLCEL.2017.12.003
Page generated: Mon Dec 14 20:56:53 2020

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