Zinc in PDB 4p35: Crystal Structure of Dj-1 with Zinc(II) Bound (Crystal I)

The structure of Crystal Structure of Dj-1 with Zinc(II) Bound (Crystal I), PDB code: 4p35 was solved by S.Tashiro, C.-X.Wu, Q.Q.Hoang, J.M.M.Caaveiro, K.Tsumoto, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.60 / 1.75
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	75.130, 75.130, 75.540, 90.00, 90.00, 120.00
R / Rfree (%)	14.2 / 17.1

The structure of Crystal Structure of Dj-1 with Zinc(II) Bound (Crystal I) also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Zinc atom in the Crystal Structure of Dj-1 with Zinc(II) Bound (Crystal I) (pdb code 4p35). 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 Crystal Structure of Dj-1 with Zinc(II) Bound (Crystal I), PDB code: 4p35:

Zinc binding site 1 out of 1 in the Crystal Structure of Dj-1 with Zinc(II) Bound (Crystal I)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Dj-1 with Zinc(II) Bound (Crystal I) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:20.5 occ:0.50 OE2 A:GLU18 2.0 16.1 1.0 SG A:CYS106 2.1 24.8 1.0 O A:HOH430 2.5 22.8 0.5 CD A:GLU18 2.9 14.1 1.0 CB A:CYS106 3.2 17.2 1.0 OE1 A:GLU18 3.3 12.9 1.0 CG A:GLU15 3.8 11.4 1.0 CD A:PRO158 3.8 11.9 1.0 N A:GLY75 3.9 13.9 1.0 O A:HOH377 4.0 41.2 1.0 CG A:PRO158 4.0 12.6 1.0 CB A:GLU15 4.1 11.2 1.0 CG A:GLU18 4.3 11.2 1.0 CA A:CYS106 4.5 14.5 1.0 CA A:GLY75 4.6 14.4 1.0 N A:PRO158 4.6 11.1 1.0 CA A:GLY157 4.7 10.8 1.0 C A:GLY74 4.8 11.8 1.0 N A:ALA107 4.8 12.3 1.0 CD A:GLU15 4.9 11.5 1.0 CA A:GLY74 4.9 10.7 1.0 CD2 A:HIS126 4.9 11.1 1.0

S.Tashiro, J.M.Caaveiro, C.X.Wu, Q.Q.Hoang, K.Tsumoto. Thermodynamic and Structural Characterization of the Specific Binding of Zn(II) to Human Protein Dj-1. Biochemistry V. 53 2218 2014.
ISSN: ISSN 1520-4995
PubMed: 24697266
DOI: 10.1021/BI500294H