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Magnesium in PDB 6fhb: Death-Associated Protein Kinase 1 (DAPK1) Catalytic and Auto- Regulatory Domains with S289A and S308E Mutations

Enzymatic activity of Death-Associated Protein Kinase 1 (DAPK1) Catalytic and Auto- Regulatory Domains with S289A and S308E Mutations

All present enzymatic activity of Death-Associated Protein Kinase 1 (DAPK1) Catalytic and Auto- Regulatory Domains with S289A and S308E Mutations:
2.7.11.1;

Protein crystallography data

The structure of Death-Associated Protein Kinase 1 (DAPK1) Catalytic and Auto- Regulatory Domains with S289A and S308E Mutations, PDB code: 6fhb was solved by A.-S.Huart, M.Wilmanns, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.01 / 1.75
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 49.507, 76.653, 108.009, 90.00, 90.00, 90.00
R / Rfree (%) 18.7 / 22.2

Other elements in 6fhb:

The structure of Death-Associated Protein Kinase 1 (DAPK1) Catalytic and Auto- Regulatory Domains with S289A and S308E Mutations also contains other interesting chemical elements:

Chlorine (Cl) 5 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Death-Associated Protein Kinase 1 (DAPK1) Catalytic and Auto- Regulatory Domains with S289A and S308E Mutations (pdb code 6fhb). 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 Death-Associated Protein Kinase 1 (DAPK1) Catalytic and Auto- Regulatory Domains with S289A and S308E Mutations, PDB code: 6fhb:

Magnesium binding site 1 out of 1 in 6fhb

Go back to Magnesium Binding Sites List in 6fhb
Magnesium binding site 1 out of 1 in the Death-Associated Protein Kinase 1 (DAPK1) Catalytic and Auto- Regulatory Domains with S289A and S308E Mutations


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Death-Associated Protein Kinase 1 (DAPK1) Catalytic and Auto- Regulatory Domains with S289A and S308E Mutations within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg407

b:46.7
occ:1.00
 O A:HOH680 2.0 45.3 1.0
OE1 A:GLU64 2.8 25.9 1.0
CE A:LYS42 3.2 48.4 1.0
NZ A:LYS42 3.2 24.3 1.0
CD A:GLU64 3.6 24.6 1.0
OE2 A:GLU64 3.7 32.1 1.0
O A:HOH520 3.9 28.1 1.0
CD1 A:ILE44 4.0 24.3 1.0
CG1 A:ILE44 4.3 23.3 1.0
CA A:GLY163 4.3 21.7 1.0
O A:HOH606 4.5 32.1 1.0
CD A:LYS42 4.6 41.0 1.0
OD1 A:ASP161 4.7 32.4 1.0
N A:GLY163 4.9 19.7 1.0
CG2 A:ILE44 5.0 24.3 1.0

Reference:

A.-S.Huart, B.Simon, J.Lubner, H.D.T.Mertens, K.Temmerman, J.-E.Hoffmann, D.I.Svergun, D.Schwartz, C.Schultz, M.Wilmanns. Molecular Mechanisms Behind Dapk Regulation: How Phosphorylation Switches Work To Be Published.
Page generated: Tue Oct 1 00:28:15 2024

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