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Sodium in PDB 6qn4: Death-Associated Protein Kinase 1 (DAPK1) Catalytic and Auto- Regulatory Domains with S289E and S308E Mutations

Enzymatic activity of Death-Associated Protein Kinase 1 (DAPK1) Catalytic and Auto- Regulatory Domains with S289E and S308E Mutations

All present enzymatic activity of Death-Associated Protein Kinase 1 (DAPK1) Catalytic and Auto- Regulatory Domains with S289E 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 S289E and S308E Mutations, PDB code: 6qn4 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) 61.23 / 2.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.374, 77.478, 99.931, 90.00, 90.00, 90.00
R / Rfree (%) 21.5 / 26.6

Sodium Binding Sites:

The binding sites of Sodium atom in the Death-Associated Protein Kinase 1 (DAPK1) Catalytic and Auto- Regulatory Domains with S289E and S308E Mutations (pdb code 6qn4). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Death-Associated Protein Kinase 1 (DAPK1) Catalytic and Auto- Regulatory Domains with S289E and S308E Mutations, PDB code: 6qn4:

Sodium binding site 1 out of 1 in 6qn4

Go back to Sodium Binding Sites List in 6qn4
Sodium binding site 1 out of 1 in the Death-Associated Protein Kinase 1 (DAPK1) Catalytic and Auto- Regulatory Domains with S289E and S308E Mutations


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Death-Associated Protein Kinase 1 (DAPK1) Catalytic and Auto- Regulatory Domains with S289E and S308E Mutations within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na412

b:63.1
occ:1.00
 O A:HOH524 2.4 65.5 1.0
O A:HOH522 3.6 53.5 1.0
OD1 A:ASN75 4.0 46.1 1.0
ND2 A:ASN125 4.3 46.5 1.0
CG A:PRO74 4.3 48.5 1.0
CB A:PRO74 4.8 46.8 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 Dec 15 12:49:56 2020

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