Zinc in PDB 3ppd: Ggvlvn Segment From Human Prostatic Acid Phosphatase Residues 260-265, Involved in Semen-Derived Enhancer of Viral Infection

The structure of Ggvlvn Segment From Human Prostatic Acid Phosphatase Residues 260-265, Involved in Semen-Derived Enhancer of Viral Infection, PDB code: 3ppd was solved by A.Zhao, M.R.Sawaya, D.Eisenberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.16 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	4.834, 17.682, 40.322, 90.00, 90.00, 90.00
R / Rfree (%)	17.8 / 21.9

The binding sites of Zinc atom in the Ggvlvn Segment From Human Prostatic Acid Phosphatase Residues 260-265, Involved in Semen-Derived Enhancer of Viral Infection (pdb code 3ppd). 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 Ggvlvn Segment From Human Prostatic Acid Phosphatase Residues 260-265, Involved in Semen-Derived Enhancer of Viral Infection, PDB code: 3ppd:

Zinc binding site 1 out of 1 in the Ggvlvn Segment From Human Prostatic Acid Phosphatase Residues 260-265, Involved in Semen-Derived Enhancer of Viral Infection


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Ggvlvn Segment From Human Prostatic Acid Phosphatase Residues 260-265, Involved in Semen-Derived Enhancer of Viral Infection within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn7 b:5.8 occ:1.00 O A:ACY8 2.0 15.7 1.0 O A:GLY1 2.1 7.4 1.0 N A:GLY1 2.2 8.4 1.0 C A:ACY8 2.8 16.1 1.0 C A:GLY1 2.9 7.9 1.0 OXT A:ACY8 2.9 15.1 1.0 CA A:GLY1 3.0 7.9 1.0 N A:GLY2 4.2 6.8 1.0 CH3 A:ACY8 4.2 16.2 1.0 O A:HOH9 4.4 17.5 1.0 CA A:GLY2 4.9 6.1 1.0

S.A.Sievers, J.Karanicolas, H.W.Chang, A.Zhao, L.Jiang, O.Zirafi, J.T.Stevens, J.Munch, D.Baker, D.Eisenberg. Structure-Based Design of Non-Natural Amino-Acid Inhibitors of Amyloid Fibril Formation. Nature V. 475 96 2011.
ISSN: ISSN 0028-0836
PubMed: 21677644
DOI: 10.1038/NATURE10154