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Magnesium in PDB 3pdt: Crystal Structure of the C-Terminal Truncated Alpha-Kinase Domain of Myosin Heavy Chain Kinase

Enzymatic activity of Crystal Structure of the C-Terminal Truncated Alpha-Kinase Domain of Myosin Heavy Chain Kinase

All present enzymatic activity of Crystal Structure of the C-Terminal Truncated Alpha-Kinase Domain of Myosin Heavy Chain Kinase:
2.7.11.7;

Protein crystallography data

The structure of Crystal Structure of the C-Terminal Truncated Alpha-Kinase Domain of Myosin Heavy Chain Kinase, PDB code: 3pdt was solved by Q.Ye, Z.Jia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.39 / 1.80
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 77.062, 83.681, 44.684, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 24.3

Other elements in 3pdt:

The structure of Crystal Structure of the C-Terminal Truncated Alpha-Kinase Domain of Myosin Heavy Chain Kinase also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the C-Terminal Truncated Alpha-Kinase Domain of Myosin Heavy Chain Kinase (pdb code 3pdt). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the C-Terminal Truncated Alpha-Kinase Domain of Myosin Heavy Chain Kinase, PDB code: 3pdt:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3pdt

Go back to Magnesium Binding Sites List in 3pdt
Magnesium binding site 1 out of 2 in the Crystal Structure of the C-Terminal Truncated Alpha-Kinase Domain of Myosin Heavy Chain Kinase


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 the C-Terminal Truncated Alpha-Kinase Domain of Myosin Heavy Chain Kinase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2

b:16.3
occ:1.00
OD1 A:ASP766 2.6 23.0 1.0
O A:HOH24 2.7 18.4 1.0
O A:PRO767 2.8 17.1 1.0
O A:HOH68 2.9 27.6 1.0
OE1 A:GLN768 3.0 19.5 1.0
CE A:MET666 3.4 19.4 1.0
CG A:ASP766 3.7 20.7 1.0
C A:PRO767 3.8 16.1 1.0
O A:HOH41 3.9 26.6 1.0
CD A:GLN768 4.0 17.9 1.0
O A:ASP766 4.0 15.9 1.0
CB A:GLN768 4.1 15.7 1.0
O A:HOH97 4.1 30.6 1.0
OD2 A:ASP766 4.2 27.2 1.0
O A:HOH209 4.2 28.2 1.0
CA A:GLN768 4.2 15.2 1.0
C A:ASP766 4.3 16.1 1.0
N A:GLN768 4.4 15.6 1.0
O A:HOH135 4.4 28.8 1.0
O A:HOH66 4.6 40.9 1.0
CG A:GLN768 4.6 16.7 1.0
CA A:ASP766 4.7 16.6 1.0
N A:PRO767 4.7 16.3 1.0
CB A:ASP766 4.8 17.5 1.0
CA A:PRO767 4.9 16.2 1.0
SD A:MET666 5.0 17.6 1.0

Magnesium binding site 2 out of 2 in 3pdt

Go back to Magnesium Binding Sites List in 3pdt
Magnesium binding site 2 out of 2 in the Crystal Structure of the C-Terminal Truncated Alpha-Kinase Domain of Myosin Heavy Chain Kinase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the C-Terminal Truncated Alpha-Kinase Domain of Myosin Heavy Chain Kinase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg3

b:20.1
occ:1.00
O A:GLY776 2.7 19.6 1.0
O A:HOH213 2.7 29.5 1.0
O A:GLY778 2.8 21.1 1.0
O A:HOH73 2.8 33.6 1.0
O A:GLY774 3.2 23.6 1.0
O A:HOH142 3.5 40.6 1.0
C A:GLY776 3.5 20.2 1.0
N A:GLY776 3.6 21.7 1.0
C A:GLY778 3.8 21.1 1.0
O A:HOH134 3.9 31.7 1.0
CB A:ASN781 3.9 17.2 1.0
O A:HOH161 3.9 48.0 1.0
CA A:GLY776 4.0 20.8 1.0
N A:GLY778 4.1 20.4 1.0
C A:LYS775 4.1 22.2 1.0
C A:GLY774 4.3 23.5 1.0
ND2 A:ASN781 4.4 17.4 1.0
CA A:GLY778 4.4 21.0 1.0
CA A:LYS775 4.4 23.2 1.0
C A:PHE777 4.5 20.1 1.0
OE2 A:GLU662 4.5 28.1 1.0
CG A:ASN781 4.6 16.7 1.0
N A:PHE777 4.6 19.7 1.0
O A:ASN781 4.7 17.9 1.0
N A:LYS775 4.8 23.0 1.0
N A:LEU779 4.8 21.4 1.0
O A:LYS775 4.8 22.2 1.0
O A:PHE777 4.9 19.9 1.0
CA A:ASN781 5.0 17.2 1.0

Reference:

S.W.Crawley, M.S.Gharaei, Q.Ye, Y.Yang, B.Raveh, N.London, O.Schueler-Furman, Z.Jia, G.P.Cote. Autophosphorylation Activates Dictyostelium Myosin II Heavy Chain Kinase A By Providing A Ligand For An Allosteric Binding Site in the {Alpha}-Kinase Domain. J.Biol.Chem. V. 286 2607 2011.
ISSN: ISSN 0021-9258
PubMed: 21071445
DOI: 10.1074/JBC.M110.177014
Page generated: Mon Dec 14 08:38:58 2020

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