Calcium in PDB 4gna: Mouse SMP30/Gnl-Xylitol Complex

All present enzymatic activity of Mouse SMP30/Gnl-Xylitol Complex:
3.1.1.17;

The structure of Mouse SMP30/Gnl-Xylitol Complex, PDB code: 4gna was solved by S.Aizawa, M.Senda, A.Harada, N.Maruyama, T.Ishida, T.Aigaki, A.Ishigami, T.Senda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	56.62 / 1.85
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	101.967, 101.967, 147.548, 90.00, 90.00, 120.00
R / Rfree (%)	16.6 / 18.4

The binding sites of Calcium atom in the Mouse SMP30/Gnl-Xylitol Complex (pdb code 4gna). 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 Mouse SMP30/Gnl-Xylitol Complex, PDB code: 4gna:

Calcium binding site 1 out of 1 in the Mouse SMP30/Gnl-Xylitol Complex


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Mouse SMP30/Gnl-Xylitol Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:19.5 occ:0.66 O5 A:XYL302 1.9 36.9 1.0 O A:HOH591 2.1 28.1 1.0 OD2 A:ASP204 2.1 26.1 1.0 OE2 A:GLU18 2.2 31.4 1.0 OD1 A:ASN154 2.2 24.0 1.0 O A:HOH592 2.4 31.7 1.0 C5 A:XYL302 3.0 30.1 1.0 CD A:GLU18 3.0 24.6 1.0 CG A:ASN154 3.1 23.0 1.0 CG A:ASP204 3.2 29.9 1.0 ND2 A:ASN154 3.2 17.4 1.0 OE1 A:GLU18 3.3 27.5 1.0 OD1 A:ASP204 3.7 25.4 1.0 ND2 A:ASN103 3.8 19.4 1.0 O A:THR246 4.1 20.1 1.0 C4 A:XYL302 4.2 41.9 1.0 CG A:GLU18 4.3 24.0 1.0 O A:HOH557 4.3 29.6 1.0 N A:GLY205 4.3 17.7 1.0 OD1 A:ASP104 4.4 26.1 1.0 CB A:ASP204 4.4 16.7 1.0 OD1 A:ASN103 4.5 21.7 1.0 C A:ASP204 4.5 17.2 1.0 CB A:ASN154 4.5 16.9 1.0 CG A:ASN103 4.5 24.3 1.0 CB A:ASP104 4.5 19.4 1.0 CG A:ASP104 4.5 27.2 1.0 O4 A:XYL302 4.6 31.3 1.0 CA A:ASP204 4.7 18.9 1.0 CA A:GLY205 4.8 20.6 1.0 CA A:ASN154 5.0 16.0 1.0 O A:ASP204 5.0 20.0 1.0 C A:THR246 5.0 17.9 1.0

S.Aizawa, M.Senda, A.Harada, N.Maruyama, T.Ishida, T.Aigaki, A.Ishigami, T.Senda. Structural Basis of the Gamma-Lactone-Ring Formation in Ascorbic Acid Biosynthesis By the Senescence Marker Protein-30/Gluconolactonase Plos One V. 8 53706 2013.
ISSN: ESSN 1932-6203
PubMed: 23349732
DOI: 10.1371/JOURNAL.PONE.0053706