Zinc in PDB 2ou7: Structure of the Catalytic Domain of Human Polo-Like Kinase 1

All present enzymatic activity of Structure of the Catalytic Domain of Human Polo-Like Kinase 1:
2.7.11.21;

The structure of Structure of the Catalytic Domain of Human Polo-Like Kinase 1, PDB code: 2ou7 was solved by Y.-H.Ding, M.Kothe, D.Kohls, S.Low, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.90 / 2.40
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	65.958, 65.958, 154.045, 90.00, 90.00, 120.00
R / Rfree (%)	20.3 / 23.5

The structure of Structure of the Catalytic Domain of Human Polo-Like Kinase 1 also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Zinc atom in the Structure of the Catalytic Domain of Human Polo-Like Kinase 1 (pdb code 2ou7). 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 the Catalytic Domain of Human Polo-Like Kinase 1, PDB code: 2ou7:

Zinc binding site 1 out of 1 in the Structure of the Catalytic Domain of Human Polo-Like Kinase 1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Catalytic Domain of Human Polo-Like Kinase 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:44.6 occ:1.00 O A:ACT502 2.0 51.1 1.0 SG A:CYS212 2.1 20.1 1.0 NE2 A:HIS93 2.2 5.2 1.0 C A:ACT502 3.0 52.9 1.0 CD2 A:HIS93 3.0 6.0 1.0 CB A:CYS212 3.3 19.1 1.0 OXT A:ACT502 3.3 53.4 1.0 CE1 A:HIS93 3.3 4.9 1.0 CG A:HIS93 4.3 6.7 1.0 CE A:LYS97 4.3 17.1 1.0 CH3 A:ACT502 4.3 52.9 1.0 ND1 A:HIS93 4.4 5.3 1.0 CA A:CYS212 4.5 19.3 1.0 CD A:LYS97 4.7 17.1 1.0 NZ A:LYS97 4.9 17.7 1.0

M.Kothe, D.Kohls, S.Low, R.Coli, A.C.Cheng, S.L.Jacques, T.L.Johnson, C.Lewis, C.Loh, J.Nonomiya, A.L.Sheils, K.A.Verdries, T.A.Wynn, C.Kuhn, Y.H.Ding. Structure of the Catalytic Domain of Human Polo-Like Kinase 1. Biochemistry V. 46 5960 2007.
ISSN: ISSN 0006-2960
PubMed: 17461553
DOI: 10.1021/BI602474J