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Magnesium in PDB 2wqn: Structure of Adp-Bound Human NEK7

Enzymatic activity of Structure of Adp-Bound Human NEK7

All present enzymatic activity of Structure of Adp-Bound Human NEK7:
2.7.11.1;

Protein crystallography data

The structure of Structure of Adp-Bound Human NEK7, PDB code: 2wqn was solved by M.W.Richards, R.Bayliss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.180 / 2.30
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 46.835, 133.108, 131.851, 90.00, 90.00, 90.00
R / Rfree (%) 19.06 / 22.05

Other elements in 2wqn:

The structure of Structure of Adp-Bound Human NEK7 also contains other interesting chemical elements:

Nickel (Ni) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Adp-Bound Human NEK7 (pdb code 2wqn). 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 Adp-Bound Human NEK7, PDB code: 2wqn:

Magnesium binding site 1 out of 1 in 2wqn

Go back to Magnesium Binding Sites List in 2wqn
Magnesium binding site 1 out of 1 in the Structure of Adp-Bound Human NEK7


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Adp-Bound Human NEK7 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1303

b:95.0
occ:1.00
O2A A:ADP1301 2.8 0.6 1.0
O1B A:ADP1301 3.0 0.1 1.0
O2B A:ADP1301 3.3 0.2 1.0
N A:GLN44 3.4 96.4 1.0
PB A:ADP1301 3.7 0.8 1.0
CA A:GLY43 4.0 89.2 1.0
CB A:GLN44 4.1 98.6 1.0
PA A:ADP1301 4.1 98.2 1.0
C A:GLY43 4.2 97.0 1.0
O3A A:ADP1301 4.3 0.2 1.0
CA A:GLN44 4.4 98.3 1.0
C5' A:ADP1301 4.9 96.1 1.0

Reference:

M.W.Richards, L.O'regan, C.Mas-Droux, J.M.Blot, J.Cheung, S.Hoelder, A.M.Fry, R.Bayliss. An Autoinhibitory Tyrosine Motif in the Cell-Cycle- Regulated NEK7 Kinase Is Released Through Binding of NEK9. Mol.Cell V. 36 560 2009.
ISSN: ISSN 1097-2765
PubMed: 19941817
DOI: 10.1016/J.MOLCEL.2009.09.038
Page generated: Mon Dec 14 07:44:49 2020

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