Zinc in PDB 8fny: Nucleotide-Bound Structure of A Functional Construct of Eukaryotic Elongation Factor 2 Kinase.

All present enzymatic activity of Nucleotide-Bound Structure of A Functional Construct of Eukaryotic Elongation Factor 2 Kinase.:
2.7.11.20;

The structure of Nucleotide-Bound Structure of A Functional Construct of Eukaryotic Elongation Factor 2 Kinase., PDB code: 8fny was solved by A.Piserchio, E.A.Isiorho, K.N.Dalby, R.Ghose, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.79 / 2.22
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	59.16, 83.352, 88.978, 65.35, 90.03, 86.47
R / Rfree (%)	20.8 / 22.9

The structure of Nucleotide-Bound Structure of A Functional Construct of Eukaryotic Elongation Factor 2 Kinase. also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Zinc atom in the Nucleotide-Bound Structure of A Functional Construct of Eukaryotic Elongation Factor 2 Kinase. (pdb code 8fny). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Nucleotide-Bound Structure of A Functional Construct of Eukaryotic Elongation Factor 2 Kinase., PDB code: 8fny:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Nucleotide-Bound Structure of A Functional Construct of Eukaryotic Elongation Factor 2 Kinase.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Nucleotide-Bound Structure of A Functional Construct of Eukaryotic Elongation Factor 2 Kinase. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn803 b:28.2 occ:1.00 NE2 A:HIS312 2.0 29.6 1.0 ND1 A:HIS260 2.1 30.8 1.0 SG A:CYS314 2.3 29.0 1.0 SG A:CYS318 2.3 30.5 1.0 CD2 A:HIS312 3.0 29.2 1.0 CE1 A:HIS260 3.0 35.8 1.0 CE1 A:HIS312 3.1 30.6 1.0 CG A:HIS260 3.1 35.6 1.0 CB A:CYS318 3.1 29.0 1.0 CB A:CYS314 3.3 26.8 1.0 CA A:CYS314 3.4 28.7 1.0 CB A:HIS260 3.4 25.2 1.0 NE2 A:HIS260 4.1 32.2 1.0 CG A:HIS312 4.1 24.8 1.0 ND1 A:HIS312 4.1 28.4 1.0 CD2 A:HIS260 4.2 28.8 1.0 N A:CYS314 4.3 35.3 1.0 CA A:CYS318 4.5 31.0 1.0 C A:CYS314 4.6 32.1 1.0 O A:HOH929 4.6 33.1 1.0 N A:ASN315 4.6 28.8 1.0 CD1 A:LEU323 4.7 31.2 1.0 CB A:LEU323 5.0 33.0 1.0 CA A:HIS260 5.0 25.8 1.0

Zinc binding site 2 out of 2 in the Nucleotide-Bound Structure of A Functional Construct of Eukaryotic Elongation Factor 2 Kinase.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Nucleotide-Bound Structure of A Functional Construct of Eukaryotic Elongation Factor 2 Kinase. within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn803 b:31.1 occ:1.00 NE2 C:HIS312 2.0 30.9 1.0 ND1 C:HIS260 2.0 29.8 1.0 SG C:CYS314 2.3 38.6 1.0 SG C:CYS318 2.3 28.0 1.0 CE1 C:HIS260 3.0 32.3 1.0 CD2 C:HIS312 3.0 31.8 1.0 CE1 C:HIS312 3.0 33.2 1.0 CG C:HIS260 3.1 35.4 1.0 CB C:CYS318 3.2 36.2 1.0 CB C:CYS314 3.3 32.7 1.0 CB C:HIS260 3.5 29.5 1.0 CA C:CYS314 3.5 36.2 1.0 NE2 C:HIS260 4.1 29.9 1.0 ND1 C:HIS312 4.1 34.0 1.0 CG C:HIS312 4.2 31.9 1.0 CD2 C:HIS260 4.2 29.9 1.0 N C:CYS314 4.3 34.0 1.0 O C:HOH930 4.4 36.3 1.0 CA C:CYS318 4.5 39.4 1.0 C C:CYS314 4.6 33.5 1.0 N C:ASN315 4.6 34.2 1.0 CD1 C:LEU323 4.7 29.5 1.0 CB C:LEU323 5.0 34.3 1.0 CA C:HIS260 5.0 24.7 1.0

A.Piserchio, K.J.Long, L.S.Browning, A.L.Bohanon, E.A.Isiorho, K.N.Dalby, R.Ghose. Adp Enhances the Allosteric Activation of Eukaryotic Elongation Factor 2 Kinase By Calmodulin. Proc.Natl.Acad.Sci.Usa V. 120 02120 2023.
ISSN: ESSN 1091-6490
PubMed: 37068230
DOI: 10.1073/PNAS.2300902120