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Zinc 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:

Magnesium (Mg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of the C-Terminal Truncated Alpha-Kinase Domain of Myosin Heavy Chain Kinase, PDB code: 3pdt:

Zinc binding site 1 out of 1 in 3pdt

Go back to Zinc Binding Sites List in 3pdt
Zinc binding site 1 out of 1 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 Zinc with other atoms in the Zn 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:Zn1

b:16.0
occ:1.00
NE2 A:HIS794 2.1 13.6 1.0
ND1 A:HIS742 2.1 14.0 1.0
SG A:CYS800 2.3 16.9 1.0
SG A:CYS796 2.3 17.7 1.0
CE1 A:HIS742 3.0 16.7 1.0
CD2 A:HIS794 3.0 12.7 1.0
CE1 A:HIS794 3.1 11.2 1.0
CB A:CYS800 3.2 17.7 1.0
CG A:HIS742 3.2 14.7 1.0
CB A:CYS796 3.3 18.3 1.0
CA A:CYS796 3.4 17.4 1.0
CB A:HIS742 3.6 13.3 1.0
N A:CYS796 4.1 18.1 1.0
NE2 A:HIS742 4.2 15.1 1.0
CG A:HIS794 4.2 14.1 1.0
ND1 A:HIS794 4.2 13.4 1.0
CD2 A:HIS742 4.3 13.8 1.0
O A:HOH105 4.4 22.5 1.0
CA A:CYS800 4.5 17.9 1.0
C A:CYS796 4.6 17.4 1.0
N A:ASN797 4.6 16.4 1.0
CD1 A:LEU805 4.7 21.7 1.0
C A:LYS795 4.7 18.3 1.0
O A:LYS795 4.8 19.0 1.0
O A:HOH258 4.8 43.2 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: Wed Dec 16 04:42:57 2020

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