Zinc in PDB 4xm5: C. Glabrata SLX1.

The structure of C. Glabrata SLX1., PDB code: 4xm5 was solved by V.Gaur, H.D.M.Wyatt, W.Komorowska, R.H.Szczepanowski, D.De Sanctis, K.M.Gorecka, S.C.West, M.Nowotny, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.73 / 2.34
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	57.486, 57.486, 183.642, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 25.1

The structure of C. Glabrata SLX1. also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Zinc atom in the C. Glabrata SLX1. (pdb code 4xm5). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the C. Glabrata SLX1., PDB code: 4xm5:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the C. Glabrata SLX1.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of C. Glabrata SLX1. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:78.2 occ:1.00 ND1 A:HIS252 2.4 68.1 1.0 SG A:CYS255 2.5 65.6 1.0 SG A:CYS219 2.6 68.3 1.0 SG A:CYS222 2.6 73.2 1.0 CB A:CYS222 2.9 73.7 1.0 CB A:CYS219 3.0 67.6 1.0 CG A:HIS252 3.3 65.1 1.0 CE1 A:HIS252 3.4 71.8 1.0 CB A:CYS255 3.4 56.1 1.0 CB A:HIS252 3.5 59.1 1.0 N A:CYS222 3.6 74.9 1.0 CA A:CYS222 3.8 77.5 1.0 N A:HIS252 4.2 61.7 1.0 CA A:HIS252 4.5 57.8 1.0 NE2 A:HIS252 4.5 72.0 1.0 CD2 A:HIS252 4.5 67.4 1.0 CA A:CYS219 4.5 82.8 1.0 C A:CYS222 4.6 84.1 1.0 C A:PHE221 4.7 76.7 1.0 N A:ASN223 4.8 89.3 1.0 CA A:CYS255 4.8 54.1 1.0 CB A:PHE221 4.8 72.3 1.0

Zinc binding site 2 out of 2 in the C. Glabrata SLX1.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of C. Glabrata SLX1. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:94.6 occ:1.00 SG A:CYS247 2.6 96.9 1.0 SG A:CYS282 2.7 80.4 1.0 SG A:CYS242 2.8 85.9 1.0 SG A:CYS279 2.8 74.7 1.0 CB A:CYS282 3.1 86.4 1.0 CB A:CYS247 3.1 86.0 1.0 CB A:CYS242 3.4 74.3 1.0 CB A:CYS279 3.7 78.2 1.0 N A:CYS282 3.7 85.5 1.0 CA A:CYS282 4.0 90.4 1.0 CB A:LYS281 4.1 92.6 1.0 C A:LYS281 4.4 95.7 1.0 CA A:CYS247 4.5 89.4 1.0 CB A:ASP244 4.6 84.4 1.0 CB A:PHE249 4.6 76.8 1.0 CA A:LYS281 4.7 94.0 1.0 CG2 A:THR284 4.8 78.3 1.0 N A:LYS281 4.8 89.8 1.0 CA A:CYS242 4.9 70.2 1.0 C A:CYS282 4.9 90.0 1.0

V.Gaur, H.D.Wyatt, W.Komorowska, R.H.Szczepanowski, D.De Sanctis, K.M.Gorecka, S.C.West, M.Nowotny. Structural and Mechanistic Analysis of the SLX1-SLX4 Endonuclease. Cell Rep 2015.
ISSN: ESSN 2211-1247
PubMed: 25753413
DOI: 10.1016/J.CELREP.2015.02.019