Zinc in PDB 4upi: Dimeric Sulfatase SPAS1 From Silicibacter Pomeroyi

The structure of Dimeric Sulfatase SPAS1 From Silicibacter Pomeroyi, PDB code: 4upi 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)	37.50 / 1.25
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	93.027, 86.029, 82.874, 90.00, 115.19, 90.00
R / Rfree (%)	14.1 / 16.3

The binding sites of Zinc atom in the Dimeric Sulfatase SPAS1 From Silicibacter Pomeroyi (pdb code 4upi). 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 Dimeric Sulfatase SPAS1 From Silicibacter Pomeroyi, PDB code: 4upi:

Zinc binding site 1 out of 1 in the Dimeric Sulfatase SPAS1 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 SPAS1 From Silicibacter Pomeroyi within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1576 b:13.1 occ:0.50 OG1 A:CYS53 1.9 13.4 0.5 OD2 A:ASP328 2.0 16.2 1.0 OD1 A:ASP13 2.0 16.6 1.0 NE2 A:HIS329 2.0 16.3 1.0 SG A:CYS53 2.5 27.3 0.5 CG A:ASP13 2.6 16.4 1.0 OD2 A:ASP13 2.7 17.6 1.0 CG A:ASP328 2.8 15.2 1.0 CE1 A:HIS329 3.0 15.8 1.0 CD2 A:HIS329 3.0 15.8 1.0 OD1 A:ASP328 3.0 16.0 1.0 CB A:CYS53 3.1 15.7 0.5 CB A:CYS53 3.3 25.0 0.5 CA A:CYS53 3.4 20.7 0.5 CA A:CYS53 3.4 15.9 0.5 OG2 A:CYS53 3.5 14.7 0.5 N A:CYS53 3.8 18.5 0.5 N A:CYS53 3.8 15.9 0.5 ND1 A:HIS329 4.0 15.7 1.0 CB A:ASP13 4.0 17.0 1.0 CG A:HIS329 4.1 14.6 1.0 NZ A:LYS101 4.2 20.3 1.0 CB A:ASP328 4.2 15.4 1.0 N A:GLN14 4.2 16.2 1.0 CD2 A:HIS234 4.3 17.8 1.0 NE A:ARG57 4.4 16.7 1.0 CA A:ASP13 4.4 16.1 1.0 NH2 A:ARG57 4.4 17.0 1.0 OE1 A:GLN14 4.6 17.0 1.0 C A:ASP13 4.7 15.7 1.0 C A:CYS53 4.8 15.7 0.5 C A:CYS53 4.8 18.4 0.5 CB A:GLN14 4.9 16.4 1.0 CA A:GLN14 4.9 16.0 1.0 C A:VAL52 4.9 16.8 1.0 CZ A:ARG57 4.9 16.6 1.0 NE2 A:HIS234 4.9 17.9 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