Zinc in PDB 4xlg: C. Glabrata SLX1 in Complex with SLX4CCD.

The structure of C. Glabrata SLX1 in Complex with SLX4CCD., PDB code: 4xlg 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)	40.00 / 1.78
Space group	P 63
Cell size a, b, c (Å), α, β, γ (°)	135.790, 135.790, 56.710, 90.00, 90.00, 120.00
R / Rfree (%)	15.8 / 18.2

The structure of C. Glabrata SLX1 in Complex with SLX4CCD. also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Zinc atom in the C. Glabrata SLX1 in Complex with SLX4CCD. (pdb code 4xlg). 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 in Complex with SLX4CCD., PDB code: 4xlg:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the C. Glabrata SLX1 in Complex with SLX4CCD.


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 in Complex with SLX4CCD. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:44.2 occ:1.00 ND1 A:HIS252 2.2 47.0 1.0 SG A:CYS219 2.3 45.3 1.0 SG A:CYS222 2.4 50.1 1.0 SG A:CYS255 2.4 46.4 1.0 CB A:CYS219 3.1 49.4 1.0 CG A:HIS252 3.1 42.8 1.0 CB A:CYS222 3.2 57.0 1.0 CE1 A:HIS252 3.2 50.9 1.0 CB A:CYS255 3.3 41.5 1.0 CB A:HIS252 3.3 40.0 1.0 N A:CYS222 3.7 52.5 1.0 N A:HIS252 4.0 40.7 1.0 CA A:CYS222 4.0 55.0 1.0 O A:HOH747 4.2 78.8 1.0 CD2 A:HIS252 4.3 45.6 1.0 CA A:HIS252 4.3 38.5 1.0 NE2 A:HIS252 4.3 48.7 1.0 CA A:CYS219 4.5 53.4 1.0 O A:HOH746 4.6 74.6 1.0 CA A:CYS255 4.7 42.6 1.0 C A:CYS222 4.7 60.3 1.0 N A:ASN223 4.8 65.2 1.0 C A:PHE221 4.9 56.1 1.0

Zinc binding site 2 out of 2 in the C. Glabrata SLX1 in Complex with SLX4CCD.


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 in Complex with SLX4CCD. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:48.5 occ:1.00 SG A:CYS279 2.4 49.0 1.0 SG A:CYS247 2.4 51.5 1.0 SG A:CYS242 2.4 45.5 1.0 SG A:CYS282 2.5 56.0 1.0 CB A:CYS279 3.2 42.3 1.0 CB A:CYS242 3.2 41.7 1.0 CB A:CYS247 3.2 51.9 1.0 CB A:CYS282 3.3 54.0 1.0 N A:CYS282 3.8 56.5 1.0 CA A:CYS282 4.1 56.9 1.0 CG2 A:THR284 4.3 48.9 1.0 CB A:PHE249 4.3 48.5 1.0 CB A:LYS281 4.5 62.7 1.0 CA A:CYS242 4.5 41.8 1.0 CA A:CYS279 4.6 44.0 1.0 CA A:CYS247 4.7 56.2 1.0 C A:CYS282 4.8 56.9 1.0 C A:LYS281 4.8 64.5 1.0 N A:TYR283 4.9 54.8 1.0 CB A:ASP244 4.9 54.7 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