Zinc in PDB 4br5: Rat NTPDASE2 in Complex with Zn Amppnp

All present enzymatic activity of Rat NTPDASE2 in Complex with Zn Amppnp:
3.6.1.5;

The structure of Rat NTPDASE2 in Complex with Zn Amppnp, PDB code: 4br5 was solved by M.Zebisch, P.Schaefer, P.Lauble, N.Straeter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.71 / 1.75
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	41.170, 69.130, 164.510, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 20

The binding sites of Zinc atom in the Rat NTPDASE2 in Complex with Zn Amppnp (pdb code 4br5). 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 Rat NTPDASE2 in Complex with Zn Amppnp, PDB code: 4br5:

Zinc binding site 1 out of 1 in the Rat NTPDASE2 in Complex with Zn Amppnp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Rat NTPDASE2 in Complex with Zn Amppnp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1502 b:32.6 occ:0.80 O1G A:ANP1501 2.1 21.2 0.8 O2B A:ANP1501 2.2 22.5 0.8 O A:HOH2006 2.3 20.0 1.0 O A:HOH2095 2.4 22.6 1.0 O A:HOH2131 2.4 25.2 1.0 O A:HOH2004 2.4 19.4 1.0 PB A:ANP1501 3.3 22.0 0.8 PG A:ANP1501 3.3 23.6 0.8 N3B A:ANP1501 3.6 18.8 0.8 O3A A:ANP1501 3.9 22.7 0.8 O3G A:ANP1501 3.9 25.5 0.8 O A:HOH2094 4.0 21.3 1.0 OE2 A:GLU165 4.0 16.4 1.0 O1A A:ANP1501 4.1 21.1 0.8 O A:HOH2256 4.1 35.6 1.0 NE1 A:TRP436 4.2 15.8 1.0 O A:HOH2132 4.2 22.3 1.0 OG1 A:THR122 4.3 16.9 1.0 OD1 A:ASP45 4.4 17.5 1.0 OD2 A:ASP45 4.4 20.0 1.0 CA A:GLY203 4.5 13.9 1.0 O2G A:ANP1501 4.5 14.6 0.8 PA A:ANP1501 4.5 21.8 0.8 OD2 A:ASP201 4.5 15.0 1.0 CD1 A:TRP436 4.6 14.7 1.0 O1B A:ANP1501 4.6 20.7 0.8 OD1 A:ASP201 4.7 15.2 1.0 CE1 A:HIS50 4.7 34.1 1.0 CA A:GLY47 4.8 17.6 1.0 O A:HOH2056 4.8 18.6 1.0 CG A:ASP45 4.9 19.6 1.0

M.Zebisch, M.Krauss, P.Schaefer, P.Lauble, N.Straeter. Crystallographic Snapshots Along the Reaction Pathway of Nucleoside Triphosphate Diphosphohydrolases Structure V. 21 1460 2013.
ISSN: ISSN 0969-2126
PubMed: 23830739
DOI: 10.1016/J.STR.2013.05.016