Magnesium in PDB 5x6i: Crystal Structure of B. Subtilis Adenylate Kinase Variant

Enzymatic activity of Crystal Structure of B. Subtilis Adenylate Kinase Variant

All present enzymatic activity of Crystal Structure of B. Subtilis Adenylate Kinase Variant:
2.7.4.3;

Protein crystallography data

The structure of Crystal Structure of B. Subtilis Adenylate Kinase Variant, PDB code: 5x6i was solved by S.Moon, E.Bae, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.739, 44.180, 100.595, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / 25.9

Other elements in 5x6i:

The structure of Crystal Structure of B. Subtilis Adenylate Kinase Variant also contains other interesting chemical elements:

Zinc (Zn) 1 atom
Calcium (Ca) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of B. Subtilis Adenylate Kinase Variant (pdb code 5x6i). 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 Crystal Structure of B. Subtilis Adenylate Kinase Variant, PDB code: 5x6i:

Magnesium binding site 1 out of 1 in 5x6i

Go back to Magnesium Binding Sites List in 5x6i
Magnesium binding site 1 out of 1 in the Crystal Structure of B. Subtilis Adenylate Kinase Variant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of B. Subtilis Adenylate Kinase Variant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg302

b:13.9
occ:1.00
O A:HOH474 2.1 24.1 1.0
O A:HOH437 2.1 26.9 1.0
O A:HOH445 2.2 35.7 1.0
O A:HOH440 2.3 24.9 1.0
O2G A:AP5303 2.3 27.5 1.0
O2B A:AP5303 2.4 25.4 1.0
PG A:AP5303 3.6 28.0 1.0
PB A:AP5303 3.7 24.8 1.0
O3B A:AP5303 4.0 29.8 1.0
N A:GLY14 4.0 24.4 1.0
O A:HOH491 4.2 44.5 1.0
O3G A:AP5303 4.2 28.5 1.0
CA A:GLY14 4.2 25.4 1.0
O1E A:AP5303 4.3 27.5 1.0
O A:HOH483 4.3 31.6 1.0
O2A A:AP5303 4.4 25.3 1.0
OD2 A:ASP84 4.4 31.6 1.0
NH2 A:ARG127 4.5 30.7 1.0
NH2 A:ARG160 4.5 27.9 1.0
OD1 A:ASP84 4.5 31.1 1.0
O3A A:AP5303 4.6 26.5 1.0
OG A:SER30 4.7 29.3 1.0
O2E A:AP5303 4.8 32.7 1.0
O1G A:AP5303 4.9 32.9 1.0
CG A:ASP84 4.9 30.5 1.0
O1B A:AP5303 4.9 23.9 1.0
NH2 A:ARG36 4.9 33.3 1.0
PA A:AP5303 4.9 27.0 1.0
PE A:AP5303 4.9 26.9 1.0
O3D A:AP5303 5.0 29.3 1.0
OD1 A:ASP33 5.0 32.3 1.0

Reference:

S.Moon, J.Kim, J.Koo, E.Bae. Structural and Mutational Analyses of Psychrophilic and Mesophilic Adenylate Kinases Highlight the Role of Hydrophobic Interactions in Protein Thermal Stability. Struct Dyn. V. 6 24702 2019.
ISSN: ESSN 2329-7778
PubMed: 31111079
DOI: 10.1063/1.5089707
Page generated: Mon Dec 14 21:26:27 2020

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