Manganese in PDB 1ino: Recombinant Inorganic Pyrophosphatase From Escherichia Coli

All present enzymatic activity of Recombinant Inorganic Pyrophosphatase From Escherichia Coli:
3.6.1.1;

The structure of Recombinant Inorganic Pyrophosphatase From Escherichia Coli, PDB code: 1ino was solved by V.Yu.Oganesyan, S.M.Avaeva, E.H.Harutyunyan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	12.00 / 2.20
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	110.400, 110.400, 76.800, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Manganese atom in the Recombinant Inorganic Pyrophosphatase From Escherichia Coli (pdb code 1ino). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Recombinant Inorganic Pyrophosphatase From Escherichia Coli, PDB code: 1ino:

Manganese binding site 1 out of 1 in the Recombinant Inorganic Pyrophosphatase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Recombinant Inorganic Pyrophosphatase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn176 b:20.7 occ:0.60 OD2 A:ASP65 2.1 32.3 1.0 OD2 A:ASP70 2.2 19.6 1.0 O A:HOH256 2.2 26.8 1.0 OD1 A:ASP102 2.2 24.7 1.0 O A:HOH276 2.6 31.4 1.0 CG A:ASP65 2.9 31.5 1.0 CG A:ASP102 2.9 22.8 1.0 CG A:ASP70 3.3 18.2 1.0 OD1 A:ASP65 3.4 32.5 1.0 OD2 A:ASP102 3.5 23.4 1.0 CB A:ASP102 3.9 23.3 1.0 CB A:ASP65 3.9 31.2 1.0 OD1 A:ASP70 4.0 18.9 1.0 NZ A:LYS104 4.0 8.3 1.0 CA A:ASP102 4.1 23.5 1.0 CB A:ASP70 4.5 16.6 1.0 C A:ASP102 4.6 23.2 1.0 O A:HOH275 4.6 30.5 1.0 OG A:SER63 4.6 23.6 1.0 O A:ALA103 4.6 17.3 1.0 O A:PRO68 4.8 19.7 1.0 O A:ASP102 4.9 24.7 1.0

S.M.Avaeva, E.V.Rodina, S.A.Kurilova, T.I.Nazarova, N.N.Vorobyeva, E.H.Harutyunyan, Oganessyan Vyu. MG2+ Activation of Escherichia Coli Inorganic Pyrophosphatase. Febs Lett. V. 377 44 1995.
ISSN: ISSN 0014-5793
PubMed: 8543015
DOI: 10.1016/0014-5793(95)01310-5