Zinc in PDB 5egy: Structure of Ligand Free Human DPP3 in Closed Form.

All present enzymatic activity of Structure of Ligand Free Human DPP3 in Closed Form.:
3.4.14.4;

The structure of Structure of Ligand Free Human DPP3 in Closed Form., PDB code: 5egy was solved by P.Kumar, V.Reithofer, M.Reisinger, T.Pavkov-Keller, S.Wallner, P.Macheroux, K.Gruber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.83 / 2.74
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	119.190, 106.206, 62.572, 90.00, 91.81, 90.00
R / Rfree (%)	20.7 / 25.4

The structure of Structure of Ligand Free Human DPP3 in Closed Form. also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Zinc atom in the Structure of Ligand Free Human DPP3 in Closed Form. (pdb code 5egy). 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 Ligand Free Human DPP3 in Closed Form., PDB code: 5egy:

Zinc binding site 1 out of 1 in the Structure of Ligand Free Human DPP3 in Closed Form.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Ligand Free Human DPP3 in Closed Form. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn801 b:90.2 occ:1.00 NE2 A:HIS450 2.0 74.5 1.0 NE2 A:HIS455 2.1 83.9 1.0 OE1 A:GLU508 2.1 72.5 1.0 O A:HOH917 2.7 74.5 1.0 CD A:GLU508 2.9 78.6 1.0 CD2 A:HIS450 2.9 79.3 1.0 OE2 A:GLU508 3.0 87.8 1.0 CD2 A:HIS455 3.0 85.9 1.0 CE1 A:HIS455 3.1 81.9 1.0 CE1 A:HIS450 3.1 73.1 1.0 CG A:HIS450 4.1 75.6 1.0 ND1 A:HIS455 4.2 82.4 1.0 CG A:HIS455 4.2 84.7 1.0 ND1 A:HIS450 4.2 72.1 1.0 CG A:GLU508 4.3 74.3 1.0 NE2 A:HIS568 4.6 79.6 1.0 OH A:TYR318 4.8 82.7 1.0 CB A:ALA511 4.9 75.7 1.0 CB A:GLU508 4.9 68.4 1.0 CD2 A:HIS568 4.9 71.7 1.0

P.Kumar, V.Reithofer, M.Reisinger, S.Wallner, T.Pavkov-Keller, P.Macheroux, K.Gruber. Substrate Complexes of Human Dipeptidyl Peptidase III Reveal the Mechanism of Enzyme Inhibition. Sci Rep V. 6 23787 2016.
ISSN: ESSN 2045-2322
PubMed: 27025154
DOI: 10.1038/SREP23787