Sodium in PDB 6s36: Crystal Structure of E. Coli Adenylate Kinase R119K Mutant

Enzymatic activity of Crystal Structure of E. Coli Adenylate Kinase R119K Mutant

All present enzymatic activity of Crystal Structure of E. Coli Adenylate Kinase R119K Mutant:
2.7.4.3;

Protein crystallography data

The structure of Crystal Structure of E. Coli Adenylate Kinase R119K Mutant, PDB code: 6s36 was solved by C.Grundstrom, P.Rogne, M.Wolf-Watz, A.E.Sauer-Eriksson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.29 / 1.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 135.690, 31.619, 53.171, 90.00, 111.86, 90.00
R / Rfree (%) 15.9 / 23.6

Other elements in 6s36:

The structure of Crystal Structure of E. Coli Adenylate Kinase R119K Mutant also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Chlorine (Cl) 3 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of E. Coli Adenylate Kinase R119K Mutant (pdb code 6s36). 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 Crystal Structure of E. Coli Adenylate Kinase R119K Mutant, PDB code: 6s36:

Sodium binding site 1 out of 1 in 6s36

Go back to Sodium Binding Sites List in 6s36
Sodium binding site 1 out of 1 in the Crystal Structure of E. Coli Adenylate Kinase R119K Mutant


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of E. Coli Adenylate Kinase R119K Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na304

b:32.2
occ:1.00
O A:GLY100 2.8 24.3 1.0
C A:GLY100 3.7 22.2 1.0
CA A:GLY100 3.8 23.4 1.0
O A:HOH590 3.8 29.3 0.5
O A:HOH521 3.8 26.9 1.0
O A:HOH447 4.3 38.0 1.0
O A:HOH621 4.7 45.8 1.0
O A:ALA99 4.8 27.2 1.0

Reference:

P.Rogne, D.Andersson, C.Grundstrom, E.Sauer-Eriksson, A.Linusson, M.Wolf-Watz. Nucleation of An Activating Conformational Change By A Cation-Pi Interaction. Biochemistry V. 58 3408 2019.
ISSN: ISSN 0006-2960
PubMed: 31339702
DOI: 10.1021/ACS.BIOCHEM.9B00538
Page generated: Tue Dec 15 12:56:58 2020

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