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Magnesium in PDB 4pf4: 1.1A X-Ray Structure of the Apo Catalytic Domain of Death-Associated Protein Kinase 1, Aa 1-277

Enzymatic activity of 1.1A X-Ray Structure of the Apo Catalytic Domain of Death-Associated Protein Kinase 1, Aa 1-277

All present enzymatic activity of 1.1A X-Ray Structure of the Apo Catalytic Domain of Death-Associated Protein Kinase 1, Aa 1-277:
2.7.11.1;

Protein crystallography data

The structure of 1.1A X-Ray Structure of the Apo Catalytic Domain of Death-Associated Protein Kinase 1, Aa 1-277, PDB code: 4pf4 was solved by K.Temmerman, B.Simon, M.Wilmanns, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.76 / 1.13
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.516, 62.005, 88.375, 90.00, 90.00, 90.00
R / Rfree (%) 11.7 / 15

Other elements in 4pf4:

The structure of 1.1A X-Ray Structure of the Apo Catalytic Domain of Death-Associated Protein Kinase 1, Aa 1-277 also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the 1.1A X-Ray Structure of the Apo Catalytic Domain of Death-Associated Protein Kinase 1, Aa 1-277 (pdb code 4pf4). 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 1.1A X-Ray Structure of the Apo Catalytic Domain of Death-Associated Protein Kinase 1, Aa 1-277, PDB code: 4pf4:

Magnesium binding site 1 out of 1 in 4pf4

Go back to Magnesium Binding Sites List in 4pf4
Magnesium binding site 1 out of 1 in the 1.1A X-Ray Structure of the Apo Catalytic Domain of Death-Associated Protein Kinase 1, Aa 1-277


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of 1.1A X-Ray Structure of the Apo Catalytic Domain of Death-Associated Protein Kinase 1, Aa 1-277 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg313

b:15.5
occ:1.00
 O A:HOH870 2.3 15.3 1.0
HZ2 A:LYS42 2.7 13.1 1.0
HZ3 A:LYS42 2.9 13.2 1.0
HB2 A:ASP161 3.0 8.7 1.0
HA A:ASP161 3.1 7.6 1.0
NZ A:LYS42 3.1 12.9 1.0
O A:HOH783 3.2 21.2 1.0
HD2 A:LYS42 3.2 10.6 1.0
O A:HOH831 3.2 18.9 1.0
O A:HOH817 3.2 39.7 1.0
HE3 A:LYS42 3.3 11.3 1.0
O A:HOH775 3.3 22.0 1.0
HD11 A:ILE160 3.4 9.3 1.0
CB A:ASP161 3.6 8.5 1.0
CE A:LYS42 3.6 10.9 1.0
CG A:ASP161 3.6 11.3 1.0
CA A:ASP161 3.7 7.7 1.0
H A:ASP161 3.8 7.2 1.0
HG22 A:VAL27 3.8 12.0 1.0
HO3 A:GOL306 3.8 15.8 1.0
CD A:LYS42 3.8 10.7 1.0
OD1 A:ASP161 3.9 11.5 1.0
HZ1 A:LYS42 4.0 12.6 1.0
OD2 A:ASP161 4.1 12.7 1.0
O3 A:GOL308 4.1 32.6 1.0
N A:ASP161 4.1 7.1 1.0
HO3 A:GOL308 4.2 30.9 1.0
CD1 A:ILE160 4.4 9.7 1.0
HB A:ILE160 4.4 7.6 1.0
O3 A:GOL306 4.4 16.1 1.0
HD3 A:LYS42 4.5 10.8 1.0
O A:HOH833 4.5 47.3 1.0
HB3 A:ASP161 4.5 8.6 1.0
HE2 A:LYS42 4.5 11.6 1.0
CG2 A:VAL27 4.6 12.1 1.0
HG3 A:LYS42 4.6 9.2 1.0
HG23 A:VAL27 4.6 11.8 1.0
O A:HOH790 4.7 9.7 1.0
HD12 A:ILE160 4.7 9.1 1.0
HG21 A:VAL27 4.7 11.7 1.0
O A:HOH800 4.8 44.3 1.0
HD13 A:ILE160 4.8 9.3 1.0
CG A:LYS42 4.8 9.2 1.0
HG13 A:ILE160 4.9 7.5 1.0

Reference:

K.Temmerman, B.Simon, M.Wilmanns. 1.1A X-Ray Structure of the Apo Catalytic Domain of Death-Associated Protein Kinase 1, Aa 1-277 To Be Published.
Page generated: Tue Aug 20 01:18:04 2024

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