Zinc in PDB 2ac5: Structure of Human MNK2 Kinase Domain Mutant D228G

All present enzymatic activity of Structure of Human MNK2 Kinase Domain Mutant D228G:
2.7.1.37;

The structure of Structure of Human MNK2 Kinase Domain Mutant D228G, PDB code: 2ac5 was solved by R.Jauch, M.C.Wahl, S.Jakel, K.Schreiter, B.Aicher, H.Jackle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 3.20
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	104.646, 104.646, 73.363, 90.00, 90.00, 120.00
R / Rfree (%)	23.8 / 30.6

The binding sites of Zinc atom in the Structure of Human MNK2 Kinase Domain Mutant D228G (pdb code 2ac5). 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 Structure of Human MNK2 Kinase Domain Mutant D228G, PDB code: 2ac5:

Zinc binding site 1 out of 1 in the Structure of Human MNK2 Kinase Domain Mutant D228G


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Human MNK2 Kinase Domain Mutant D228G within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn386 b:1.0 occ:1.00 CB A:CYS303 2.0 0.1 1.0 SG A:CYS311 2.1 0.2 1.0 SG A:CYS303 2.3 0.1 1.0 SG A:CYS314 2.5 0.4 1.0 SG A:CYS299 2.6 0.7 1.0 CB A:CYS311 2.7 0.6 1.0 CB A:CYS314 3.1 0.1 1.0 CA A:CYS303 3.4 0.8 1.0 NE1 A:TRP305 3.5 0.0 1.0 N A:GLY304 4.0 0.3 1.0 N A:CYS314 4.0 0.7 1.0 CD1 A:TRP305 4.0 0.9 1.0 CA A:CYS314 4.1 0.9 1.0 CA A:CYS311 4.2 0.1 1.0 C A:CYS303 4.3 0.5 1.0 N A:CYS303 4.3 0.9 1.0 CB A:CYS299 4.3 0.5 1.0 O A:CYS311 4.5 0.4 1.0 CE2 A:TRP305 4.7 0.9 1.0 N A:CYS299 4.7 0.2 1.0 C A:CYS311 4.7 0.0 1.0 C A:ASP302 5.0 0.7 1.0

R.Jauch, S.Jakel, C.Netter, K.Schreiter, B.Aicher, H.Jackle, M.C.Wahl. Crystal Structures of the MNK2 Kinase Domain Reveal An Inhibitory Conformation and A Zinc Binding Site. Structure V. 13 1559 2005.
ISSN: ISSN 0969-2126
PubMed: 16216586
DOI: 10.1016/J.STR.2005.07.013