Calcium in PDB 1qe5: Purine Nucleoside Phosphorylase From Cellulomonas Sp. in Complex with Phosphate

All present enzymatic activity of Purine Nucleoside Phosphorylase From Cellulomonas Sp. in Complex with Phosphate:
2.4.2.1;

The structure of Purine Nucleoside Phosphorylase From Cellulomonas Sp. in Complex with Phosphate, PDB code: 1qe5 was solved by J.Tebbe, A.Bzowska, B.Wielgus-Kutrowska, W.Schroeder, Z.Kazimierczuk, D.Shugar, W.Saenger, G.Koellner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.00 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	64.120, 108.900, 119.300, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 26

The binding sites of Calcium atom in the Purine Nucleoside Phosphorylase From Cellulomonas Sp. in Complex with Phosphate (pdb code 1qe5). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Purine Nucleoside Phosphorylase From Cellulomonas Sp. in Complex with Phosphate, PDB code: 1qe5:

Calcium binding site 1 out of 1 in the Purine Nucleoside Phosphorylase From Cellulomonas Sp. in Complex with Phosphate


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Purine Nucleoside Phosphorylase From Cellulomonas Sp. in Complex with Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca300 b:16.5 occ:1.00 O B:HOH452 2.3 20.9 1.0 O B:HOH542 2.4 29.9 1.0 OE1 B:GLU128 2.5 26.6 1.0 O B:GLY126 2.6 15.7 1.0 O B:HOH453 2.6 28.5 1.0 O B:HOH478 2.6 36.9 1.0 CD B:GLU128 3.4 27.3 1.0 OE2 B:GLU128 3.6 30.9 1.0 C B:GLY126 3.7 18.3 1.0 O B:HIS38 4.2 16.3 1.0 CA B:GLY126 4.2 18.2 1.0 N B:GLU128 4.7 17.9 1.0 OD1 B:ASP39 4.7 24.4 1.0 N B:ALA127 4.8 18.0 1.0 CG B:GLU128 4.8 22.4 1.0 O B:HOH526 4.9 36.9 1.0 CA B:ALA127 5.0 17.9 1.0

J.Tebbe, A.Bzowska, B.Wielgus-Kutrowska, W.Schroder, Z.Kazimierczuk, D.Shugar, W.Saenger, G.Koellner. Crystal Structure of the Purine Nucleoside Phosphorylase (Pnp) From Cellulomonas Sp. and Its Implication For the Mechanism of Trimeric Pnps. J.Mol.Biol. V. 294 1239 1999.
ISSN: ISSN 0022-2836
PubMed: 10600382
DOI: 10.1006/JMBI.1999.3327