Calcium in PDB 8gm4: Functional Construct of the Eukaryotic Elongation Factor 2 Kinase Bound to An Atp-Competitive Inhibitor

All present enzymatic activity of Functional Construct of the Eukaryotic Elongation Factor 2 Kinase Bound to An Atp-Competitive Inhibitor:
2.7.11.20;

The structure of Functional Construct of the Eukaryotic Elongation Factor 2 Kinase Bound to An Atp-Competitive Inhibitor, PDB code: 8gm4 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)	47.73 / 2.12
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	80.544, 60.684, 88.704, 90, 111.1, 90
R / Rfree (%)	20.7 / 23.8

The structure of Functional Construct of the Eukaryotic Elongation Factor 2 Kinase Bound to An Atp-Competitive Inhibitor also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Calcium atom in the Functional Construct of the Eukaryotic Elongation Factor 2 Kinase Bound to An Atp-Competitive Inhibitor (pdb code 8gm4). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Functional Construct of the Eukaryotic Elongation Factor 2 Kinase Bound to An Atp-Competitive Inhibitor, PDB code: 8gm4:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Functional Construct of the Eukaryotic Elongation Factor 2 Kinase Bound to An Atp-Competitive Inhibitor


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Functional Construct of the Eukaryotic Elongation Factor 2 Kinase Bound to An Atp-Competitive Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca201 b:35.7 occ:1.00 OD1 B:ASP95 2.2 35.6 1.0 OD1 B:ASP93 2.3 34.5 1.0 OD1 B:ASN97 2.3 35.2 1.0 O B:TYR99 2.4 41.0 1.0 OE2 B:GLU104 2.4 36.1 1.0 OE1 B:GLU104 2.4 38.6 1.0 O A:HOH1034 2.5 38.8 1.0 CD B:GLU104 2.7 36.4 1.0 CG B:ASP95 3.2 36.2 1.0 CG B:ASN97 3.3 27.1 1.0 CG B:ASP93 3.5 40.2 1.0 C B:TYR99 3.5 36.1 1.0 OD2 B:ASP95 3.7 36.8 1.0 N B:ASN97 4.1 31.2 1.0 ND2 B:ASN97 4.1 26.6 1.0 N B:TYR99 4.2 36.0 1.0 N B:ASP95 4.2 37.7 1.0 CB B:ASN97 4.2 36.8 1.0 CG B:GLU104 4.2 40.0 1.0 CB B:ASP95 4.2 33.6 1.0 OD2 B:ASP93 4.3 35.4 1.0 CA B:ASP93 4.3 40.8 1.0 CA B:TYR99 4.4 32.7 1.0 C B:ASP93 4.4 36.2 1.0 CB B:ASP93 4.5 34.7 1.0 N B:GLY96 4.5 34.9 1.0 N B:ILE100 4.5 33.7 1.0 N B:LYS94 4.5 38.0 1.0 OD2 A:ASP208 4.6 34.6 1.0 CA B:ASP95 4.6 33.7 1.0 CA B:ASN97 4.6 36.2 1.0 CA B:ILE100 4.6 36.7 1.0 N B:SER101 4.7 40.5 1.0 C B:ASP95 4.8 28.2 1.0 CB B:TYR99 4.8 38.7 1.0 NZ A:LYS192 4.8 32.6 1.0 N B:GLY98 4.8 34.1 1.0 C B:ASN97 4.9 36.3 1.0 O B:ASP93 5.0 40.8 1.0

Calcium binding site 2 out of 2 in the Functional Construct of the Eukaryotic Elongation Factor 2 Kinase Bound to An Atp-Competitive Inhibitor


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Functional Construct of the Eukaryotic Elongation Factor 2 Kinase Bound to An Atp-Competitive Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca202 b:47.4 occ:1.00 OD1 B:ASP131 2.2 53.4 1.0 O B:GLN135 2.3 42.2 1.0 O B:HOH309 2.3 47.2 1.0 OD1 B:ASP133 2.3 47.7 1.0 OD1 B:ASP129 2.3 50.0 1.0 OE1 B:GLU140 2.5 41.3 1.0 OE2 B:GLU140 2.7 41.8 1.0 CD B:GLU140 3.0 52.2 1.0 CG B:ASP133 3.1 45.2 1.0 CG B:ASP131 3.4 57.1 1.0 C B:GLN135 3.4 43.7 1.0 CG B:ASP129 3.4 45.7 1.0 OD2 B:ASP133 3.5 51.8 1.0 OD2 B:ASP131 4.0 64.4 1.0 CA B:ASP129 4.1 53.1 1.0 N B:GLN135 4.2 48.2 1.0 N B:VAL136 4.2 41.6 1.0 N B:ASP133 4.2 53.5 1.0 OD2 B:ASP129 4.2 55.1 1.0 CB B:ASP129 4.3 41.0 1.0 CA B:VAL136 4.3 41.7 1.0 CB B:ASP133 4.3 52.1 1.0 N B:ASP131 4.4 51.8 1.0 CA B:GLN135 4.4 45.3 1.0 N B:ASN137 4.4 39.4 1.0 CB B:ASP131 4.4 50.1 1.0 CG B:GLU140 4.5 41.1 1.0 N B:GLY132 4.6 52.5 1.0 N B:ILE130 4.6 48.9 1.0 C B:ASP129 4.6 56.7 1.0 CA B:ASP133 4.7 46.8 1.0 CA B:ASP131 4.8 44.4 1.0 C B:VAL136 4.8 39.4 1.0 ND2 B:ASN137 4.9 38.2 1.0 C B:ASP131 4.9 50.6 1.0 N B:GLY134 4.9 41.7 1.0 O B:HOH317 4.9 53.6 1.0 CG B:ASN137 5.0 42.8 1.0 CB B:GLN135 5.0 48.1 1.0

A.Piserchio, E.A.Isiorho, K.N.Dalby, R.Ghose. Structure of the Complex Between Calmodulin and A Functional Construct of Eukaryotic Elongation Factor 2 Kinase Bound to An Atp-Competitive Inhibitor. J.Biol.Chem. 04813 2023.
ISSN: ESSN 1083-351X
PubMed: 37172726
DOI: 10.1016/J.JBC.2023.104813