Zinc in PDB 4yxp: The Structure of the Folded Domain of the Signature Multifunctional Protein ICP27 From Herpes Simplex Virus-1 Reveals An Intertwined Dimer.

The structure of The Structure of the Folded Domain of the Signature Multifunctional Protein ICP27 From Herpes Simplex Virus-1 Reveals An Intertwined Dimer., PDB code: 4yxp was solved by R.B.Tunnicliffe, M.Schacht, C.W.Levy, T.A.Jowitt, R.M.Sandri-Goldin, A.P.Golovanov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.55 / 1.92
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	99.330, 133.620, 44.970, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / 20.3

The binding sites of Zinc atom in the The Structure of the Folded Domain of the Signature Multifunctional Protein ICP27 From Herpes Simplex Virus-1 Reveals An Intertwined Dimer. (pdb code 4yxp). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Structure of the Folded Domain of the Signature Multifunctional Protein ICP27 From Herpes Simplex Virus-1 Reveals An Intertwined Dimer., PDB code: 4yxp:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The Structure of the Folded Domain of the Signature Multifunctional Protein ICP27 From Herpes Simplex Virus-1 Reveals An Intertwined Dimer.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Structure of the Folded Domain of the Signature Multifunctional Protein ICP27 From Herpes Simplex Virus-1 Reveals An Intertwined Dimer. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:24.5 occ:0.71 NE2 A:HIS479 2.1 33.2 1.0 SG A:CYS400 2.3 31.4 1.0 SG A:CYS488 2.3 31.6 1.0 SG A:CYS483 2.4 33.1 1.0 CD2 A:HIS479 3.0 32.0 1.0 CE1 A:HIS479 3.1 32.8 1.0 CB A:CYS488 3.2 30.7 1.0 CB A:CYS400 3.3 29.3 1.0 CB A:CYS483 3.3 35.2 1.0 O A:HOH874 3.7 44.4 1.0 CG A:HIS479 4.1 30.8 1.0 ND1 A:HIS479 4.2 31.3 1.0 O A:HOH857 4.3 34.2 1.0 O A:HOH867 4.4 40.5 1.0 CA A:CYS400 4.5 28.5 1.0 C A:CYS400 4.6 26.5 1.0 O A:HOH840 4.6 35.6 1.0 CA A:CYS488 4.7 28.4 1.0 N A:TYR401 4.7 24.9 1.0 CA A:CYS483 4.7 37.6 1.0 CB A:SER485 4.8 32.1 1.0 O A:HOH820 4.9 39.0 1.0 O A:CYS400 5.0 26.4 1.0

Zinc binding site 2 out of 2 in the The Structure of the Folded Domain of the Signature Multifunctional Protein ICP27 From Herpes Simplex Virus-1 Reveals An Intertwined Dimer.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Structure of the Folded Domain of the Signature Multifunctional Protein ICP27 From Herpes Simplex Virus-1 Reveals An Intertwined Dimer. within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn601 b:27.2 occ:0.84 NE2 B:HIS479 2.1 33.8 1.0 SG B:CYS400 2.3 35.8 1.0 SG B:CYS483 2.3 32.6 1.0 SG B:CYS488 2.4 32.3 1.0 CD2 B:HIS479 3.0 33.8 1.0 CE1 B:HIS479 3.1 34.8 1.0 CB B:CYS483 3.2 34.7 1.0 CB B:CYS400 3.3 32.5 1.0 CB B:CYS488 3.3 31.3 1.0 ND1 B:HIS479 4.1 34.4 1.0 CG B:HIS479 4.1 34.3 1.0 O B:HOH836 4.3 29.8 1.0 O B:HOH816 4.4 42.1 1.0 CA B:CYS400 4.5 30.5 1.0 C B:CYS400 4.5 30.0 1.0 CA B:CYS483 4.7 38.3 1.0 O B:HOH826 4.8 33.4 1.0 CA B:CYS488 4.8 29.2 1.0 N B:TYR401 4.8 29.7 1.0 O B:CYS400 4.9 30.8 1.0 CB B:SER485 4.9 32.9 1.0

R.B.Tunnicliffe, M.Schacht, C.Levy, T.A.Jowitt, R.M.Sandri-Goldin, A.P.Golovanov. The Structure of the Folded Domain From the Signature Multifunctional Protein ICP27 From Herpes Simplex Virus-1 Reveals An Intertwined Dimer. Sci Rep V. 5 11234 2015.
ISSN: ESSN 2045-2322
PubMed: 26062451
DOI: 10.1038/SREP11234