Zinc in PDB 1ps3: Golgi Alpha-Mannosidase II in Complex with Kifunensine

All present enzymatic activity of Golgi Alpha-Mannosidase II in Complex with Kifunensine:
3.2.1.114;

The structure of Golgi Alpha-Mannosidase II in Complex with Kifunensine, PDB code: 1ps3 was solved by N.Shah, D.A.Kuntz, D.R.Rose, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	69.089, 109.803, 138.896, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 22.2

The binding sites of Zinc atom in the Golgi Alpha-Mannosidase II in Complex with Kifunensine (pdb code 1ps3). 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 Golgi Alpha-Mannosidase II in Complex with Kifunensine, PDB code: 1ps3:

Zinc binding site 1 out of 1 in the Golgi Alpha-Mannosidase II in Complex with Kifunensine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Golgi Alpha-Mannosidase II in Complex with Kifunensine within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1601 b:8.9 occ:1.00 OD1 A:ASP204 2.1 9.8 1.0 NE2 A:HIS90 2.2 8.8 1.0 NE2 A:HIS471 2.2 8.7 1.0 OD1 A:ASP92 2.2 9.2 1.0 O3 A:KIF1501 2.4 14.8 1.0 O2 A:KIF1501 2.4 14.1 1.0 CD2 A:HIS471 3.1 8.5 1.0 C2 A:KIF1501 3.1 17.0 1.0 CD2 A:HIS90 3.1 8.3 1.0 CG A:ASP204 3.1 8.8 1.0 CG A:ASP92 3.1 8.5 1.0 CE1 A:HIS90 3.1 8.7 1.0 C3 A:KIF1501 3.2 16.1 1.0 CE1 A:HIS471 3.2 7.4 1.0 OD2 A:ASP92 3.4 11.1 1.0 CB A:ASP204 3.5 8.9 1.0 OD2 A:ASP472 4.0 8.8 1.0 C1 A:KIF1501 4.1 18.0 1.0 C4 A:KIF1501 4.2 16.0 1.0 OD2 A:ASP204 4.2 9.3 1.0 ND1 A:HIS90 4.3 7.8 1.0 CG A:HIS471 4.3 7.0 1.0 CG A:HIS90 4.3 7.9 1.0 ND1 A:HIS471 4.3 6.8 1.0 NE2 A:HIS470 4.4 9.4 1.0 CB A:ASP92 4.5 7.7 1.0 O A:HOH1694 4.6 9.6 1.0 OH A:TYR269 4.8 13.8 1.0 O4 A:KIF1501 5.0 13.1 1.0

N.Shah, D.A.Kuntz, D.R.Rose. Comparison of Kifunensine and 1-Deoxymannojirimycin Binding to Class I and II Alpha-Mannosidases Demonstrates Different Saccharide Distortions in Inverting and Retaining Catalytic Mechanisms Biochemistry V. 42 13812 2003.
ISSN: ISSN 0006-2960
PubMed: 14636047
DOI: 10.1021/BI034742R