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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 8gm4:

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

Calcium (Ca) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc was determined in the Functional Construct of the Eukaryotic Elongation Factor 2 Kinase Bound to An Atp-Competitive Inhibitor, PDB code: 8gm4:

Zinc binding site 1 out of 1 in 8gm4

Go back to Zinc Binding Sites List in 8gm4
Zinc binding site 1 out of 1 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 Zinc with other atoms in the Zn 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
A:Zn803

b:42.7
occ:1.00
 NE2 A:HIS312 2.0 37.5 1.0
ND1 A:HIS260 2.0 42.0 1.0
SG A:CYS318 2.3 46.2 1.0
SG A:CYS314 2.3 42.6 1.0
CE1 A:HIS260 2.9 50.6 1.0
CE1 A:HIS312 3.0 42.8 1.0
CD2 A:HIS312 3.0 44.5 1.0
CB A:CYS318 3.1 50.2 1.0
CG A:HIS260 3.1 50.3 1.0
CB A:CYS314 3.3 34.2 1.0
CA A:CYS314 3.4 48.0 1.0
CB A:HIS260 3.5 41.5 1.0
NE2 A:HIS260 4.1 48.4 1.0
ND1 A:HIS312 4.1 35.5 1.0
CG A:HIS312 4.1 36.2 1.0
CD2 A:HIS260 4.2 45.2 1.0
N A:CYS314 4.2 43.2 1.0
O A:HOH1057 4.3 50.0 1.0
CA A:CYS318 4.4 46.1 1.0
C A:CYS314 4.6 53.0 1.0
N A:ASN315 4.6 46.5 1.0
CD1 A:LEU323 4.8 42.2 1.0
C A:ALA313 4.9 48.4 1.0
CB A:LEU323 5.0 46.8 1.0

Reference:

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
Page generated: Wed Oct 30 20:56:53 2024

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