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Magnesium in PDB 6zje: Crystal Structure of Human Adenylate Kinase 3, AK3, in Complex with Inhibitor AP5A

Enzymatic activity of Crystal Structure of Human Adenylate Kinase 3, AK3, in Complex with Inhibitor AP5A

All present enzymatic activity of Crystal Structure of Human Adenylate Kinase 3, AK3, in Complex with Inhibitor AP5A:
2.7.4.10;

Protein crystallography data

The structure of Crystal Structure of Human Adenylate Kinase 3, AK3, in Complex with Inhibitor AP5A, PDB code: 6zje 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) 40.62 / 1.48
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.716, 62.639, 50.162, 90.00, 108.01, 90.00
R / Rfree (%) 14.3 / 18.4

Other elements in 6zje:

The structure of Crystal Structure of Human Adenylate Kinase 3, AK3, in Complex with Inhibitor AP5A also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms
Sodium (Na) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Human Adenylate Kinase 3, AK3, in Complex with Inhibitor AP5A (pdb code 6zje). 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 Human Adenylate Kinase 3, AK3, in Complex with Inhibitor AP5A, PDB code: 6zje:

Magnesium binding site 1 out of 1 in 6zje

Go back to Magnesium Binding Sites List in 6zje
Magnesium binding site 1 out of 1 in the Crystal Structure of Human Adenylate Kinase 3, AK3, in Complex with Inhibitor AP5A


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 Human Adenylate Kinase 3, AK3, in Complex with Inhibitor AP5A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg405

b:36.8
occ:1.00
O A:HOH631 2.2 48.6 1.0
O A:HOH607 2.4 31.0 1.0
O A:HOH541 2.4 33.7 1.0
O A:HOH665 2.4 44.4 1.0
O1G A:AP5401 2.5 84.2 0.7
O A:HOH731 2.5 49.5 1.0
O A:HOH545 2.6 38.8 1.0
PG A:AP5401 3.7 84.4 0.7
O2G A:AP5401 3.9 84.3 0.7
O A:HOH766 3.9 35.3 0.4
O A:HOH503 4.5 25.5 0.5
CA A:GLY21 4.6 23.3 1.0
O1B A:AP5401 4.7 92.6 0.7
OG A:SER24 4.7 23.2 0.4
CE1 A:HIS35 4.7 28.3 1.0
O1D A:AP5401 4.8 79.0 0.7
O3B A:AP5401 4.8 88.6 0.7
O A:GLY21 4.8 21.3 1.0
O3G A:AP5401 4.8 82.0 0.7
OD2 A:ASP90 4.8 28.6 1.0
OD2 A:ASP40 4.9 36.8 1.0

Reference:

P.Rogne, B.Dulko-Smith, J.Goodman, M.Rosselin, C.Grundstrom, C.Hedberg, K.Nam, A.E.Sauer-Eriksson, M.Wolf-Watz. Structural Basis For Gtp Versus Atp Selectivity in the Nmp Kinase AK3. Biochemistry V. 59 3570 2020.
ISSN: ISSN 0006-2960
PubMed: 32822537
DOI: 10.1021/ACS.BIOCHEM.0C00549
Page generated: Wed Aug 13 22:10:43 2025

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