Zinc in PDB 4upl: Dimeric Sulfatase SPAS2 From Silicibacter Pomeroyi

The structure of Dimeric Sulfatase SPAS2 From Silicibacter Pomeroyi, PDB code: 4upl was solved by S.Jonas, B.Van Loo, F.Hollfelder, M.Hyvonen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.46 / 1.81
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	101.330, 105.120, 110.440, 90.00, 90.00, 90.00
R / Rfree (%)	16.3 / 20.8

The binding sites of Zinc atom in the Dimeric Sulfatase SPAS2 From Silicibacter Pomeroyi (pdb code 4upl). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Dimeric Sulfatase SPAS2 From Silicibacter Pomeroyi, PDB code: 4upl:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Dimeric Sulfatase SPAS2 From Silicibacter Pomeroyi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Dimeric Sulfatase SPAS2 From Silicibacter Pomeroyi within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1553 b:16.8 occ:0.70 OD2 A:ASP326 2.1 16.7 1.0 NE2 A:HIS327 2.2 13.6 1.0 OD1 A:ASP9 2.2 16.6 1.0 SG A:CYS49 2.4 33.7 1.0 CG A:ASP9 2.7 15.0 1.0 OD2 A:ASP9 2.7 17.8 1.0 CG A:ASP326 2.9 12.3 1.0 CD2 A:HIS327 3.0 15.1 1.0 OD1 A:ASP326 3.0 9.5 1.0 CE1 A:HIS327 3.1 14.1 1.0 CB A:CYS49 3.2 20.4 1.0 CA A:CYS49 3.4 18.5 1.0 N A:CYS49 3.9 15.2 1.0 CG A:HIS327 4.1 10.6 1.0 ND1 A:HIS327 4.1 11.9 1.0 CB A:ASP9 4.1 11.8 1.0 NZ A:LYS97 4.2 18.9 1.0 CB A:ASP326 4.3 12.0 1.0 N A:GLN10 4.4 9.8 1.0 NE A:ARG53 4.4 11.5 1.0 CD2 A:HIS232 4.5 18.2 1.0 CA A:ASP9 4.5 12.2 1.0 NH2 A:ARG53 4.6 10.0 1.0 OE1 A:GLN10 4.6 16.3 1.0 O A:HOH2064 4.6 33.5 1.0 C A:CYS49 4.7 15.8 1.0 C A:ASP9 4.8 11.3 1.0 C A:ILE48 4.9 17.6 1.0 CE A:LYS339 4.9 20.0 1.0 CZ A:ARG53 5.0 13.4 1.0

Zinc binding site 2 out of 2 in the Dimeric Sulfatase SPAS2 From Silicibacter Pomeroyi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Dimeric Sulfatase SPAS2 From Silicibacter Pomeroyi within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1553 b:15.7 occ:0.70 OD2 C:ASP326 2.1 12.9 1.0 OD1 C:ASP9 2.1 15.3 1.0 NE2 C:HIS327 2.2 16.6 1.0 SG C:CYS49 2.4 33.0 1.0 CG C:ASP9 2.7 15.9 1.0 OD2 C:ASP9 2.7 17.2 1.0 CG C:ASP326 2.9 13.0 1.0 CD2 C:HIS327 3.0 15.2 1.0 OD1 C:ASP326 3.1 13.8 1.0 CE1 C:HIS327 3.1 16.3 1.0 CB C:CYS49 3.2 21.0 1.0 CA C:CYS49 3.5 16.6 1.0 N C:CYS49 4.0 18.2 1.0 CB C:ASP9 4.1 13.2 1.0 ND1 C:HIS327 4.1 13.1 1.0 CG C:HIS327 4.1 13.5 1.0 NZ C:LYS97 4.3 17.7 1.0 CB C:ASP326 4.3 9.5 1.0 N C:GLN10 4.4 12.8 1.0 CD2 C:HIS232 4.4 17.1 1.0 NE C:ARG53 4.5 12.4 1.0 CA C:ASP9 4.5 11.3 1.0 OE1 C:GLN10 4.6 13.6 1.0 NH2 C:ARG53 4.6 12.1 1.0 C C:CYS49 4.8 17.5 1.0 C C:ASP9 4.8 11.7 1.0 CE C:LYS339 4.9 15.8 1.0 C C:ILE48 4.9 15.3 1.0 O C:HOH2067 4.9 29.7 1.0 CA C:GLN10 5.0 12.3 1.0

B.Van Loo, C.D.Bayer, G.Fischer, S.Jonas, E.Valkov, M.F.Mohamed, A.Vorobieva, C.Dutruel, M.Hyvonen, F.Hollfelder. Balancing Specificity and Promiscuity in Enzyme Evolution: Multidimensional Activity Transitions in the Alkaline Phosphatase Superfamily. J.Am.Chem.Soc. V. 141 370 2019.
ISSN: ESSN 1520-5126
PubMed: 30497259
DOI: 10.1021/JACS.8B10290