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Magnesium in PDB 4qbg: Crystal Structure of A Stable Adenylate Kinase Variant AKLSE4

Enzymatic activity of Crystal Structure of A Stable Adenylate Kinase Variant AKLSE4

All present enzymatic activity of Crystal Structure of A Stable Adenylate Kinase Variant AKLSE4:
2.7.4.3;

Protein crystallography data

The structure of Crystal Structure of A Stable Adenylate Kinase Variant AKLSE4, PDB code: 4qbg 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) 49.32 / 1.37
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 68.817, 71.020, 45.555, 90.00, 95.13, 90.00
R / Rfree (%) 17.9 / 22

Other elements in 4qbg:

The structure of Crystal Structure of A Stable Adenylate Kinase Variant AKLSE4 also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of A Stable Adenylate Kinase Variant AKLSE4 (pdb code 4qbg). 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 A Stable Adenylate Kinase Variant AKLSE4, PDB code: 4qbg:

Magnesium binding site 1 out of 1 in 4qbg

Go back to Magnesium Binding Sites List in 4qbg
Magnesium binding site 1 out of 1 in the Crystal Structure of A Stable Adenylate Kinase Variant AKLSE4


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 A Stable Adenylate Kinase Variant AKLSE4 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg303

b:19.4
occ:1.00
O2G B:AP5302 2.0 17.9 1.0
O B:HOH438 2.1 19.3 1.0
O B:HOH424 2.1 18.4 1.0
O B:HOH456 2.1 21.4 1.0
O B:HOH428 2.1 19.6 1.0
O2B B:AP5302 2.1 16.8 1.0
PG B:AP5302 3.3 18.2 1.0
PB B:AP5302 3.3 17.1 1.0
O3B B:AP5302 3.6 17.8 1.0
O B:HOH441 3.9 31.2 1.0
O2A B:AP5302 4.0 18.8 1.0
O1E B:AP5302 4.1 18.5 1.0
O B:HOH439 4.1 40.4 1.0
N B:GLY14 4.1 14.2 1.0
O B:HOH408 4.1 23.0 1.0
O1D B:AP5302 4.2 20.2 1.0
OD2 B:ASP84 4.3 16.3 1.0
O3G B:AP5302 4.3 19.2 1.0
OD1 B:ASP84 4.3 14.4 1.0
O3D B:AP5302 4.3 19.1 1.0
CA B:GLY14 4.3 14.0 1.0
O1G B:AP5302 4.3 20.5 1.0
O3A B:AP5302 4.4 17.7 1.0
O1B B:AP5302 4.4 17.2 1.0
PE B:AP5302 4.5 17.7 1.0
PD B:AP5302 4.6 19.3 1.0
O2E B:AP5302 4.6 18.0 1.0
PA B:AP5302 4.7 18.0 1.0
CG B:ASP84 4.7 13.9 1.0
OD1 B:ASP33 4.8 17.7 1.0
OG B:SER30 4.9 14.9 1.0
O1A B:AP5302 4.9 17.6 1.0
CB B:LYS13 5.0 15.7 1.0
O B:HOH560 5.0 37.2 1.0

Reference:

S.Moon, R.M.Bannen, T.J.Rutkoski, G.N.Phillips, E.Bae. Effectiveness and Limitations of Local Structural Entropy Optimization in the Thermal Stabilization of Mesophilic and Thermophilic Adenylate Kinases Proteins V. 82 2014.
ISSN: ESSN 1097-0134
DOI: 10.1002/PROT.24627
Page generated: Tue Aug 20 01:52:03 2024

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