Zinc in PDB 4zmf: Phosphorylated Aspartate in the Crystal Structure of the Alpha-Kinase Domain of Myosin-II Heavy Chain Kinase A

All present enzymatic activity of Phosphorylated Aspartate in the Crystal Structure of the Alpha-Kinase Domain of Myosin-II Heavy Chain Kinase A:
2.7.11.7;

The structure of Phosphorylated Aspartate in the Crystal Structure of the Alpha-Kinase Domain of Myosin-II Heavy Chain Kinase A, PDB code: 4zmf 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)	79.06 / 2.39
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	83.098, 109.960, 79.485, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 21.7

The binding sites of Zinc atom in the Phosphorylated Aspartate in the Crystal Structure of the Alpha-Kinase Domain of Myosin-II Heavy Chain Kinase A (pdb code 4zmf). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Phosphorylated Aspartate in the Crystal Structure of the Alpha-Kinase Domain of Myosin-II Heavy Chain Kinase A, PDB code: 4zmf:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Phosphorylated Aspartate in the Crystal Structure of the Alpha-Kinase Domain of Myosin-II Heavy Chain Kinase A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Phosphorylated Aspartate in the Crystal Structure of the Alpha-Kinase Domain of Myosin-II Heavy Chain Kinase A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn903 b:27.8 occ:1.00 NE2 A:HIS794 2.1 28.4 1.0 ND1 A:HIS742 2.2 29.8 1.0 SG A:CYS800 2.2 27.1 1.0 SG A:CYS796 2.4 30.4 1.0 CE1 A:HIS794 3.0 27.4 1.0 CE1 A:HIS742 3.1 31.9 1.0 CB A:CYS800 3.1 29.0 1.0 CG A:HIS742 3.2 29.8 1.0 CD2 A:HIS794 3.2 27.6 1.0 CB A:CYS796 3.3 30.9 1.0 CA A:CYS796 3.4 32.0 1.0 CB A:HIS742 3.5 28.2 1.0 N A:CYS796 4.1 34.0 1.0 ND1 A:HIS794 4.2 25.2 1.0 NE2 A:HIS742 4.2 30.5 1.0 CD2 A:HIS742 4.3 32.0 1.0 CG A:HIS794 4.3 27.5 1.0 O A:HOH1010 4.5 41.2 1.0 CA A:CYS800 4.5 29.9 1.0 C A:CYS796 4.5 33.9 1.0 N A:ASN797 4.6 29.8 1.0 CD1 A:LEU805 4.6 28.9 1.0 C A:LYS795 4.7 38.8 1.0 O A:LYS795 4.8 39.5 1.0

Zinc binding site 2 out of 2 in the Phosphorylated Aspartate in the Crystal Structure of the Alpha-Kinase Domain of Myosin-II Heavy Chain Kinase A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Phosphorylated Aspartate in the Crystal Structure of the Alpha-Kinase Domain of Myosin-II Heavy Chain Kinase A within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn903 b:31.7 occ:1.00 NE2 B:HIS794 2.0 26.6 1.0 ND1 B:HIS742 2.1 30.5 1.0 SG B:CYS800 2.3 33.0 1.0 SG B:CYS796 2.4 39.8 1.0 CE1 B:HIS794 2.9 28.3 1.0 CE1 B:HIS742 3.0 29.5 1.0 CG B:HIS742 3.1 27.1 1.0 CD2 B:HIS794 3.1 30.1 1.0 CB B:CYS800 3.2 32.6 1.0 CB B:CYS796 3.4 38.8 1.0 CA B:CYS796 3.5 39.4 1.0 CB B:HIS742 3.5 26.2 1.0 ND1 B:HIS794 4.1 28.0 1.0 NE2 B:HIS742 4.1 28.1 1.0 N B:CYS796 4.2 37.4 1.0 CD2 B:HIS742 4.2 27.6 1.0 CG B:HIS794 4.2 30.5 1.0 CA B:CYS800 4.5 32.4 1.0 C B:CYS796 4.6 42.8 1.0 N B:ASN797 4.7 40.9 1.0 CD1 B:LEU805 4.7 32.1 1.0 C B:LYS795 4.8 41.3 1.0 O B:LYS795 4.8 42.2 1.0

Y.Yang, Q.Ye, Z.Jia, G.P.Cote. Characterization of the Catalytic and Nucleotide Binding Properties of the Alpha-Kinase Domain of Dictyostelium Myosin-II Heavy Chain Kinase A. J.Biol.Chem. V. 290 23935 2015.
ISSN: ESSN 1083-351X
PubMed: 26260792
DOI: 10.1074/JBC.M115.672410