Zinc in PDB 6g84: Structure of CDC14 Bound to CBK1 Pxl Motif

All present enzymatic activity of Structure of CDC14 Bound to CBK1 Pxl Motif:
3.1.3.48;

The structure of Structure of CDC14 Bound to CBK1 Pxl Motif, PDB code: 6g84 was solved by S.Mouilleron, M.Kataria, F.Uhlmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	55.29 / 2.47
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	174.500, 73.930, 83.530, 90.00, 114.27, 90.00
R / Rfree (%)	22.6 / 27

The structure of Structure of CDC14 Bound to CBK1 Pxl Motif also contains other interesting chemical elements:

Calcium

(Ca)

2 atoms

The binding sites of Zinc atom in the Structure of CDC14 Bound to CBK1 Pxl Motif (pdb code 6g84). 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 CDC14 Bound to CBK1 Pxl Motif, PDB code: 6g84:

Zinc binding site 1 out of 1 in the Structure of CDC14 Bound to CBK1 Pxl Motif


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of CDC14 Bound to CBK1 Pxl Motif within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn402 b:91.6 occ:1.00 OE2 B:GLU193 2.0 0.2 1.0 NE2 B:HIS238 2.1 97.7 1.0 NE2 B:HIS206 2.1 0.2 1.0 ND1 B:HIS195 2.2 86.1 1.0 CE1 B:HIS238 2.7 90.1 1.0 CE1 B:HIS195 2.9 86.3 1.0 CE1 B:HIS206 3.0 0.8 1.0 CD B:GLU193 3.0 0.5 1.0 CD2 B:HIS206 3.3 0.9 1.0 CD2 B:HIS238 3.3 87.5 1.0 OE1 B:GLU193 3.4 0.1 1.0 CG B:HIS195 3.4 86.1 1.0 CD2 B:LEU207 3.8 77.0 1.0 ND1 B:HIS238 3.9 88.5 1.0 CB B:HIS195 4.0 85.4 1.0 NE2 B:HIS195 4.1 85.9 1.0 ND1 B:HIS206 4.1 0.7 1.0 CA B:HIS195 4.2 86.7 1.0 CG B:HIS238 4.2 84.5 1.0 CG B:HIS206 4.3 0.2 1.0 CG B:GLU193 4.3 92.0 1.0 CD2 B:HIS195 4.4 86.2 1.0 CB B:ASN235 4.7 57.5 1.0 CD B:PRO196 4.7 87.3 1.0 CG B:LEU207 4.9 76.3 1.0 CB B:GLU193 5.0 86.1 1.0 N B:HIS195 5.0 93.2 1.0

M.Kataria, S.Mouilleron, M.H.Seo, C.Corbi-Verge, P.M.Kim, F.Uhlmann. A Pxl Motif Promotes Timely Cell Cycle Substrate Dephosphorylation By the CDC14 Phosphatase. Nat. Struct. Mol. Biol. V. 25 1093 2018.
ISSN: ESSN 1545-9985
PubMed: 30455435
DOI: 10.1038/S41594-018-0152-3