Calcium in PDB 5jbf: 4,6-Alpha-Glucanotransferase Gtfb (D1015N Mutant) From Lactobacillus Reuteri 121 Complexed with Maltopentaose

All present enzymatic activity of 4,6-Alpha-Glucanotransferase Gtfb (D1015N Mutant) From Lactobacillus Reuteri 121 Complexed with Maltopentaose:
2.4.1.5;

The structure of 4,6-Alpha-Glucanotransferase Gtfb (D1015N Mutant) From Lactobacillus Reuteri 121 Complexed with Maltopentaose, PDB code: 5jbf was solved by T.Pijning, B.W.Dijkstra, Y.Bai, J.Gangoiti-Munecas, L.Dijkhuizen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.02 / 2.19
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	219.484, 58.139, 150.382, 90.00, 114.36, 90.00
R / Rfree (%)	19.4 / 23.8

The binding sites of Calcium atom in the 4,6-Alpha-Glucanotransferase Gtfb (D1015N Mutant) From Lactobacillus Reuteri 121 Complexed with Maltopentaose (pdb code 5jbf). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the 4,6-Alpha-Glucanotransferase Gtfb (D1015N Mutant) From Lactobacillus Reuteri 121 Complexed with Maltopentaose, PDB code: 5jbf:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the 4,6-Alpha-Glucanotransferase Gtfb (D1015N Mutant) From Lactobacillus Reuteri 121 Complexed with Maltopentaose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of 4,6-Alpha-Glucanotransferase Gtfb (D1015N Mutant) From Lactobacillus Reuteri 121 Complexed with Maltopentaose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1704 b:28.3 occ:1.00 OE2 A:GLU969 2.2 27.9 1.0 OD1 A:ASP975 2.3 28.2 1.0 O A:GLU969 2.3 29.5 1.0 O A:ASN1019 2.4 29.9 1.0 OD1 A:ASN1483 2.4 27.4 1.0 O A:HOH1861 2.5 19.6 1.0 OD2 A:ASP975 2.8 26.6 1.0 CG A:ASP975 2.9 27.6 1.0 CD A:GLU969 3.2 29.5 1.0 C A:GLU969 3.4 28.9 1.0 CG A:ASN1483 3.5 27.3 1.0 C A:ASN1019 3.6 29.5 1.0 CG A:GLU969 3.7 29.4 1.0 CA A:GLU969 4.1 29.4 1.0 O A:ASN1483 4.1 28.5 1.0 ND2 A:ASN1483 4.2 26.7 1.0 OE1 A:GLU969 4.3 30.0 1.0 CB A:ASP975 4.4 28.1 1.0 O A:HOH1835 4.4 27.8 1.0 CA A:ILE1020 4.4 29.7 1.0 CB A:ASN1019 4.4 30.2 1.0 N A:ILE1020 4.4 29.3 1.0 CG2 A:ILE1020 4.4 29.9 1.0 N A:LEU970 4.5 28.9 1.0 CB A:GLU969 4.5 29.7 1.0 O A:HOH1922 4.5 29.5 1.0 CA A:ASN1019 4.6 30.1 1.0 CB A:ASN1483 4.6 28.1 1.0 O A:ILE976 4.7 29.0 1.0 CA A:LEU970 4.7 29.1 1.0 CA A:ASN1483 4.7 28.6 1.0 ND2 A:ASN1574 4.7 30.4 1.0 C A:ASN1483 4.8 28.9 1.0

Calcium binding site 2 out of 2 in the 4,6-Alpha-Glucanotransferase Gtfb (D1015N Mutant) From Lactobacillus Reuteri 121 Complexed with Maltopentaose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of 4,6-Alpha-Glucanotransferase Gtfb (D1015N Mutant) From Lactobacillus Reuteri 121 Complexed with Maltopentaose within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1704 b:33.9 occ:1.00 O B:HOH1926 2.2 31.7 1.0 OE2 B:GLU969 2.2 37.3 1.0 OD1 B:ASP975 2.3 36.5 1.0 O B:GLU969 2.3 35.4 1.0 O B:ASN1019 2.4 35.5 1.0 OD1 B:ASN1483 2.4 37.4 1.0 OD2 B:ASP975 2.8 36.7 1.0 CG B:ASP975 2.9 36.4 1.0 CD B:GLU969 3.2 37.3 1.0 C B:GLU969 3.4 35.6 1.0 CG B:ASN1483 3.5 38.1 1.0 C B:ASN1019 3.6 35.0 1.0 CG B:GLU969 3.7 37.2 1.0 CA B:GLU969 4.1 35.6 1.0 O B:ASN1483 4.2 37.7 1.0 ND2 B:ASN1483 4.2 38.8 1.0 O B:HOH1868 4.3 24.5 1.0 OE1 B:GLU969 4.3 37.1 1.0 CB B:ASP975 4.4 36.6 1.0 CA B:ILE1020 4.4 35.2 1.0 CG2 B:ILE1020 4.4 35.2 1.0 N B:ILE1020 4.4 35.2 1.0 CB B:ASN1019 4.4 35.7 1.0 CB B:GLU969 4.5 36.8 1.0 N B:LEU970 4.5 35.9 1.0 CA B:ASN1019 4.6 35.1 1.0 O B:HOH1895 4.6 41.1 1.0 CB B:ASN1483 4.6 37.9 1.0 O B:ILE976 4.6 37.7 1.0 CA B:ASN1483 4.7 38.0 1.0 CA B:LEU970 4.7 36.3 1.0 ND2 B:ASN1574 4.7 35.2 1.0 C B:ASN1483 4.9 38.8 1.0

Y.Bai, J.Gangoiti, B.W.Dijkstra, L.Dijkhuizen, T.Pijning. Crystal Structure of 4,6-Alpha-Glucanotransferase Supports Diet-Driven Evolution of GH70 Enzymes From Alpha-Amylases in Oral Bacteria. Structure V. 25 231 2017.
ISSN: ISSN 1878-4186
PubMed: 28065507
DOI: 10.1016/J.STR.2016.11.023