Zinc in PDB 1v8n: Crystal Structure Analysis of the Adp-Ribose Pyrophosphatase Complexed with Zn

All present enzymatic activity of Crystal Structure Analysis of the Adp-Ribose Pyrophosphatase Complexed with Zn:
3.6.1.13;

The structure of Crystal Structure Analysis of the Adp-Ribose Pyrophosphatase Complexed with Zn, PDB code: 1v8n was solved by S.Yoshiba, T.Ooga, N.Nakagawa, T.Shibata, Y.Inoue, S.Yokoyama, S.Kuramitsu, R.Masui, Riken Structural Genomics/Proteomics Initiative (Rsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.93 / 1.74
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	49.860, 49.860, 118.310, 90.00, 90.00, 120.00
R / Rfree (%)	22.1 / 25.6

The binding sites of Zinc atom in the Crystal Structure Analysis of the Adp-Ribose Pyrophosphatase Complexed with Zn (pdb code 1v8n). 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 Crystal Structure Analysis of the Adp-Ribose Pyrophosphatase Complexed with Zn, PDB code: 1v8n:

Zinc binding site 1 out of 1 in the Crystal Structure Analysis of the Adp-Ribose Pyrophosphatase Complexed with Zn


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure Analysis of the Adp-Ribose Pyrophosphatase Complexed with Zn within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn300 b:78.4 occ:1.00 O A:HOH323 2.3 22.2 1.0 OE2 A:GLU82 2.3 18.9 1.0 O A:HOH322 2.4 44.9 1.0 O A:HOH317 2.6 50.3 1.0 OE1 A:GLU82 2.8 21.4 1.0 CD A:GLU82 2.9 17.0 1.0 OE2 A:GLU86 3.6 18.6 1.0 O A:HOH321 3.9 20.5 1.0 CG A:GLU86 4.2 15.8 1.0 O A:ALA66 4.2 15.4 1.0 CD A:GLU86 4.2 17.6 1.0 OE1 A:GLU85 4.2 19.2 1.0 CG A:GLU82 4.4 17.8 1.0 NH1 A:ARG81 4.6 16.9 1.0 O A:HOH350 4.7 25.8 1.0 CA A:GLY67 4.7 14.4 1.0

S.Yoshiba, T.Ooga, N.Nakagawa, T.Shibata, Y.Inoue, S.Yokoyama, S.Kuramitsu, R.Masui. Structural Insights Into the Thermus Thermophilus Adp-Ribose Pyrophosphatase Mechanism Via Crystal Structures with the Bound Substrate and Metal J.Biol.Chem. V. 279 37163 2004.
ISSN: ISSN 0021-9258
PubMed: 15210687
DOI: 10.1074/JBC.M403817200