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Magnesium in PDB 2v62: Structure of Vaccinia-Related Kinase 2

Enzymatic activity of Structure of Vaccinia-Related Kinase 2

All present enzymatic activity of Structure of Vaccinia-Related Kinase 2:
2.7.11.1;

Protein crystallography data

The structure of Structure of Vaccinia-Related Kinase 2, PDB code: 2v62 was solved by G.Bunkoczi, J.Eswaran, C.Cooper, O.Fedorov, T.Keates, P.Rellos, E.Salah, P.Savitsky, E.Ugochukwu, F.Von Delft, C.H.Arrowsmith, A.Edwards, M.Sundstrom, J.Weigelt, S.Knapp, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.7
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 70.655, 157.532, 56.288, 90.00, 90.00, 90.00
R / Rfree (%) 20.1 / 23.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Vaccinia-Related Kinase 2 (pdb code 2v62). 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 Vaccinia-Related Kinase 2, PDB code: 2v62:

Magnesium binding site 1 out of 1 in 2v62

Go back to Magnesium Binding Sites List in 2v62
Magnesium binding site 1 out of 1 in the Structure of Vaccinia-Related Kinase 2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Vaccinia-Related Kinase 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1331

b:28.9
occ:1.00
O A:ARG207 2.2 30.8 1.0
O A:HOH1084 2.3 42.4 1.0
O A:HOH1085 2.6 26.8 1.0
C A:ARG207 3.1 28.1 1.0
CA A:ARG207 3.9 25.5 1.0
N A:LYS208 3.9 28.5 1.0
CA A:LYS208 4.2 34.1 1.0
N A:GLY209 4.4 28.7 1.0
O A:PRO206 4.6 30.1 1.0
CB A:ARG207 4.7 30.8 1.0
C A:LYS208 4.7 32.3 1.0
O A:GLY209 4.8 26.7 1.0

Reference:

E.D.Scheeff, J.Eswaran, G.Bunkoczi, S.Knapp, G.Manning. Structure of the Pseudokinase VRK3 Reveals A Degraded Catalytic Site, A Highly Conserved Kinase Fold, and A Putative Regulatory Binding Site. Structure V. 17 128 2009.
ISSN: ISSN 0969-2126
PubMed: 19141289
DOI: 10.1016/J.STR.2008.10.018
Page generated: Wed Aug 14 04:59:17 2024

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