Calcium in PDB 8fo6: Nucleotide-Free Structure of A Functional Construct of Eukaryotic Elongation Factor 2 Kinase.

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

The structure of Nucleotide-Free Structure of A Functional Construct of Eukaryotic Elongation Factor 2 Kinase., PDB code: 8fo6 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)	47.52 / 2.55
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	77.527, 58.901, 88.394, 90, 109.67, 90
R / Rfree (%)	21.7 / 23.1

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

Zinc

(Zn)

1 atom

The binding sites of Calcium atom in the Nucleotide-Free Structure of A Functional Construct of Eukaryotic Elongation Factor 2 Kinase. (pdb code 8fo6). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Nucleotide-Free Structure of A Functional Construct of Eukaryotic Elongation Factor 2 Kinase., PDB code: 8fo6:
Jump to Calcium binding site number: 1; 2;

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


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Nucleotide-Free Structure of A Functional Construct of Eukaryotic Elongation Factor 2 Kinase. within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca201 b:40.0 occ:1.00 OD1 B:ASP95 2.1 45.8 1.0 O B:TYR99 2.3 44.0 1.0 O A:HOH929 2.3 37.6 1.0 OD1 B:ASN97 2.3 37.8 1.0 OD1 B:ASP93 2.3 44.8 1.0 OE2 B:GLU104 2.3 44.5 1.0 OE1 B:GLU104 2.6 39.9 1.0 CD B:GLU104 2.8 43.2 1.0 CG B:ASP95 3.2 50.6 1.0 CG B:ASN97 3.3 41.5 1.0 C B:TYR99 3.5 45.5 1.0 CG B:ASP93 3.5 47.3 1.0 OD2 B:ASP95 3.8 47.3 1.0 N B:TYR99 4.1 48.1 1.0 N B:ASN97 4.1 45.5 1.0 ND2 B:ASN97 4.1 38.5 1.0 N B:ASP95 4.2 47.5 1.0 CA B:ASP93 4.2 45.4 1.0 CB B:ASN97 4.2 39.9 1.0 CG B:GLU104 4.3 40.7 1.0 CA B:TYR99 4.3 45.2 1.0 OD2 B:ASP93 4.3 49.3 1.0 C B:ASP93 4.3 48.7 1.0 CB B:ASP95 4.4 49.4 1.0 CB B:ASP93 4.4 47.1 1.0 N B:LYS94 4.4 44.7 1.0 N B:GLY96 4.5 49.4 1.0 N B:ILE100 4.5 45.6 1.0 OD2 A:ASP208 4.5 46.5 1.0 CA B:ASP95 4.6 48.0 1.0 CA B:ASN97 4.6 45.3 1.0 CA B:ILE100 4.6 48.2 1.0 N B:SER101 4.7 46.8 1.0 C B:ASP95 4.7 50.2 1.0 CB B:TYR99 4.7 44.2 1.0 N B:GLY98 4.8 45.5 1.0 NZ A:LYS192 4.9 43.1 1.0 O B:ASP93 4.9 46.4 1.0 C B:ASN97 5.0 48.3 1.0

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


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Nucleotide-Free Structure of A Functional Construct of Eukaryotic Elongation Factor 2 Kinase. within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca202 b:55.7 occ:1.00 OD1 B:ASP129 2.2 63.1 1.0 O B:GLN135 2.4 54.1 1.0 OE1 B:GLU140 2.5 64.1 1.0 OD1 B:ASP133 2.5 63.1 1.0 O B:HOH302 2.6 52.2 1.0 OE2 B:GLU140 2.7 63.6 1.0 OD1 B:ASP131 2.7 63.6 1.0 OD2 B:ASP131 2.7 67.4 1.0 CD B:GLU140 2.9 61.7 1.0 CG B:ASP131 3.0 59.5 1.0 CG B:ASP129 3.4 63.8 1.0 CG B:ASP133 3.4 61.9 1.0 C B:GLN135 3.4 56.1 1.0 OD2 B:ASP133 3.8 63.9 1.0 CA B:ASP129 4.0 59.0 1.0 CB B:ASP129 4.2 55.1 1.0 N B:VAL136 4.2 53.0 1.0 OD2 B:ASP129 4.2 65.3 1.0 CA B:VAL136 4.2 52.5 1.0 N B:ASP133 4.3 59.8 1.0 N B:ASP131 4.3 55.6 1.0 N B:GLN135 4.3 58.5 1.0 N B:ASN137 4.3 52.2 1.0 ND2 B:ASN137 4.3 53.1 1.0 CB B:ASP131 4.4 62.6 1.0 N B:GLY132 4.4 62.7 1.0 N B:ILE130 4.4 64.9 1.0 CA B:GLN135 4.4 57.8 1.0 CG B:GLU140 4.4 55.3 1.0 C B:ASP129 4.5 62.4 1.0 CB B:ASP133 4.6 58.5 1.0 CA B:ASP131 4.8 55.5 1.0 C B:VAL136 4.8 51.5 1.0 CG B:ASN137 4.8 54.0 1.0 CA B:ASP133 4.9 60.7 1.0 C B:ASP131 4.9 58.0 1.0 CB B:GLN135 5.0 57.2 1.0 O B:ALA128 5.0 62.1 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