Calcium in PDB 4gn7: Mouse SMP30/Gnl

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

The structure of Mouse SMP30/Gnl, PDB code: 4gn7 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)	51.34 / 1.95
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	102.678, 102.678, 147.817, 90.00, 90.00, 120.00
R / Rfree (%)	18.5 / 21.5

The binding sites of Calcium atom in the Mouse SMP30/Gnl (pdb code 4gn7). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Mouse SMP30/Gnl, PDB code: 4gn7:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Mouse SMP30/Gnl


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:32.6 occ:1.00 O A:HOH576 2.1 26.8 1.0 OD2 A:ASP204 2.2 30.4 1.0 OE2 A:GLU18 2.2 36.0 1.0 O A:HOH577 2.3 31.0 1.0 O A:HOH578 2.4 34.3 1.0 OD1 A:ASN154 2.4 29.4 1.0 CD A:GLU18 3.0 32.2 1.0 OE1 A:GLU18 3.2 34.2 1.0 CG A:ASP204 3.2 30.6 1.0 CG A:ASN154 3.2 30.7 1.0 ND2 A:ASN154 3.4 23.5 1.0 OD1 A:ASP204 3.7 29.9 1.0 ND2 A:ASN103 3.8 21.3 1.0 O A:THR246 4.1 23.7 1.0 O A:HOH485 4.2 29.9 1.0 CG A:GLU18 4.2 27.4 1.0 N A:GLY205 4.4 23.9 1.0 OD1 A:ASP104 4.4 30.8 1.0 OD1 A:ASN103 4.5 24.0 1.0 CG A:ASN103 4.5 26.1 1.0 CB A:ASP204 4.5 20.1 1.0 CB A:ASP104 4.5 26.4 1.0 CG A:ASP104 4.6 30.4 1.0 C A:ASP204 4.6 23.4 1.0 CB A:ASN154 4.7 24.7 1.0 CA A:ASP204 4.8 21.4 1.0 CA A:GLY205 4.9 22.3 1.0 C A:THR246 5.0 21.1 1.0

Calcium binding site 2 out of 2 in the Mouse SMP30/Gnl


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Mouse SMP30/Gnl within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca301 b:47.4 occ:1.00 OD1 B:ASN154 2.2 36.8 1.0 OD2 B:ASP204 2.2 29.8 1.0 O B:HOH528 2.3 35.4 1.0 OE2 B:GLU18 2.3 37.6 1.0 O B:HOH553 2.4 44.1 1.0 CD B:GLU18 3.0 35.4 1.0 CG B:ASN154 3.1 40.4 1.0 OE1 B:GLU18 3.2 36.8 1.0 CG B:ASP204 3.3 32.6 1.0 ND2 B:ASN154 3.4 35.9 1.0 ND2 B:ASN103 3.7 34.0 1.0 O B:HOH512 3.8 41.0 1.0 OD1 B:ASP204 3.8 30.5 1.0 O B:THR246 4.1 24.9 1.0 CG B:GLU18 4.3 28.2 1.0 OD1 B:ASN103 4.4 32.6 1.0 CB B:ASP104 4.4 32.4 1.0 N B:GLY205 4.4 24.3 1.0 CG B:ASN103 4.4 35.1 1.0 OD1 B:ASP104 4.5 39.8 1.0 CB B:ASN154 4.5 26.0 1.0 CB B:ASP204 4.6 24.6 1.0 C B:ASP204 4.6 28.5 1.0 CG B:ASP104 4.6 35.4 1.0 CA B:ASP204 4.8 25.1 1.0 O B:HOH559 4.8 43.8 1.0 CA B:GLY205 4.9 26.4 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