Potassium in PDB 1mas: Purine Nucleoside Hydrolase

All present enzymatic activity of Purine Nucleoside Hydrolase:
3.2.2.1;

The structure of Purine Nucleoside Hydrolase, PDB code: 1mas was solved by M.Degano, D.N.Gopaul, G.Scapin, V.L.Schramm, J.C.Sacchettini, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	99.00 / 2.50
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	63.840, 131.530, 90.100, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Potassium atom in the Purine Nucleoside Hydrolase (pdb code 1mas). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Purine Nucleoside Hydrolase, PDB code: 1mas:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Purine Nucleoside Hydrolase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Purine Nucleoside Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ A:K900 b:14.2 occ:1.00 OD1 A:ASP10 2.4 11.7 1.0 OD1 A:ASP15 2.5 7.0 1.0 O A:HOH902 2.5 27.6 1.0 OD2 A:ASP15 2.6 1.8 1.0 O A:THR126 2.7 6.6 1.0 OD2 A:ASP242 2.7 14.5 1.0 CG A:ASP15 2.9 1.3 1.0 CG A:ASP10 3.4 3.5 1.0 C A:THR126 3.6 2.7 1.0 CG A:ASP242 3.7 9.5 1.0 OD2 A:ASP10 3.9 12.8 1.0 OD1 A:ASP242 3.9 19.1 1.0 OG1 A:THR126 4.1 7.7 1.0 O A:ASP10 4.2 14.5 1.0 CA A:GLY127 4.3 3.2 1.0 N A:GLY127 4.3 3.7 1.0 N A:ASP10 4.3 11.5 1.0 CB A:THR126 4.3 1.0 1.0 CB A:ASP15 4.4 4.0 1.0 CA A:THR126 4.6 1.9 1.0 C A:ASP10 4.6 15.4 1.0 OD1 A:ASN168 4.7 1.0 1.0 CB A:ASP10 4.7 2.5 1.0 ND2 A:ASN168 4.7 3.0 1.0 CA A:ASP10 4.8 6.3 1.0 N A:ASP15 4.9 2.4 1.0

Potassium binding site 2 out of 2 in the Purine Nucleoside Hydrolase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Purine Nucleoside Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ B:K933 b:43.6 occ:1.00 OD1 B:ASP15 2.3 10.6 1.0 O B:THR126 2.5 33.2 1.0 OD1 B:ASP10 2.6 52.4 1.0 OD2 B:ASP242 2.6 55.7 1.0 CG B:ASP15 3.1 22.6 1.0 OD2 B:ASP15 3.2 23.4 1.0 CG B:ASP10 3.4 47.6 1.0 OD2 B:ASP10 3.4 41.4 1.0 CG B:ASP242 3.6 45.3 1.0 O B:HOH950 3.6 42.2 1.0 C B:THR126 3.7 29.4 1.0 O B:HOH956 3.9 29.4 1.0 OD1 B:ASP242 4.0 43.5 1.0 CA B:GLY127 4.5 12.9 1.0 N B:GLY127 4.5 17.4 1.0 CB B:THR126 4.5 11.8 1.0 CB B:ASP15 4.5 29.6 1.0 O B:ASP10 4.5 38.9 1.0 OD1 B:ASN168 4.6 31.7 1.0 N B:ASP15 4.6 31.8 1.0 ND2 B:ASN168 4.7 9.2 1.0 CA B:THR126 4.7 16.1 1.0 OG1 B:THR126 4.7 17.8 1.0 CB B:ASP10 4.8 30.7 1.0 C B:ASP10 4.9 39.8 1.0 N B:ASP10 4.9 18.0 1.0 CB B:ASP242 4.9 16.0 1.0 CA B:ASP15 5.0 29.4 1.0

M.Degano, D.N.Gopaul, G.Scapin, V.L.Schramm, J.C.Sacchettini. Three-Dimensional Structure of the Inosine-Uridine Nucleoside N-Ribohydrolase From Crithidia Fasciculata. Biochemistry V. 35 5971 1996.
ISSN: ISSN 0006-2960
PubMed: 8634238
DOI: 10.1021/BI952999M