Magnesium in PDB 6sh6: Crystal Structure of the Human Deah-Helicase DHX15 in Complex with the Nkrf G-Patch Bound to Adp

Enzymatic activity of Crystal Structure of the Human Deah-Helicase DHX15 in Complex with the Nkrf G-Patch Bound to Adp

All present enzymatic activity of Crystal Structure of the Human Deah-Helicase DHX15 in Complex with the Nkrf G-Patch Bound to Adp:
3.6.4.13;

Protein crystallography data

The structure of Crystal Structure of the Human Deah-Helicase DHX15 in Complex with the Nkrf G-Patch Bound to Adp, PDB code: 6sh6 was solved by S.Jonas, M.K.Studer, L.Ivanovic, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.40 / 1.85
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 82.855, 91.212, 212.839, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 24.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Human Deah-Helicase DHX15 in Complex with the Nkrf G-Patch Bound to Adp (pdb code 6sh6). 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 Human Deah-Helicase DHX15 in Complex with the Nkrf G-Patch Bound to Adp, PDB code: 6sh6:

Magnesium binding site 1 out of 1 in 6sh6

Go back to Magnesium Binding Sites List in 6sh6
Magnesium binding site 1 out of 1 in the Crystal Structure of the Human Deah-Helicase DHX15 in Complex with the Nkrf G-Patch Bound to Adp


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 Human Deah-Helicase DHX15 in Complex with the Nkrf G-Patch Bound to Adp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg803

b:33.9
occ:1.00
 O A:HOH972 2.0 31.8 1.0
OG1 A:THR167 2.0 34.8 1.0
O A:HOH944 2.0 33.4 1.0
O2B A:ADP801 2.0 32.9 1.0
O A:HOH995 2.1 34.0 1.0
O A:HOH1115 2.3 38.7 1.0
CB A:THR167 3.0 37.5 1.0
PB A:ADP801 3.3 37.8 1.0
O3B A:ADP801 3.6 36.9 1.0
OE1 A:GLU261 3.8 42.3 1.0
OD2 A:ASP260 3.8 35.2 1.0
N A:THR167 3.9 36.1 1.0
O A:SER427 3.9 40.8 1.0
O2A A:ADP801 4.0 38.4 1.0
CA A:THR167 4.1 36.7 1.0
CG2 A:THR167 4.1 37.5 1.0
OD1 A:ASP260 4.3 33.4 1.0
O1B A:ADP801 4.3 37.9 1.0
O3A A:ADP801 4.3 35.3 1.0
CG A:ASP260 4.5 34.6 1.0
CD A:GLU261 4.5 41.4 1.0
C A:SER427 4.6 42.8 1.0
NZ A:LYS166 4.6 33.5 1.0
PA A:ADP801 4.7 38.2 1.0
CE A:LYS166 4.7 32.3 1.0
O A:THR426 4.8 45.5 1.0
O A:HOH1112 4.8 35.6 1.0
OE1 A:GLN192 4.8 35.3 1.0
CG A:GLU261 4.8 37.5 1.0
CB A:LYS166 4.9 32.6 1.0
CA A:SER427 5.0 41.8 1.0

Reference:

M.K.Studer, L.Ivanovic, M.E.Weber, S.Marti, S.Jonas. Structural Basis For Deah-Helicase Activation By G-Patch Proteins. Proc.Natl.Acad.Sci.Usa V. 117 7159 2020.
ISSN: ESSN 1091-6490
PubMed: 32179686
DOI: 10.1073/PNAS.1913880117
Page generated: Tue Dec 15 00:04:21 2020

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