Calcium in PDB 5jbe: 4,6-Alpha-Glucanotransferase Gtfb From Lactobacillus Reuteri 121 Complexed with An Isomalto-Maltopentasaccharide

All present enzymatic activity of 4,6-Alpha-Glucanotransferase Gtfb From Lactobacillus Reuteri 121 Complexed with An Isomalto-Maltopentasaccharide:
2.4.1.5;

The structure of 4,6-Alpha-Glucanotransferase Gtfb From Lactobacillus Reuteri 121 Complexed with An Isomalto-Maltopentasaccharide, PDB code: 5jbe 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)	46.16 / 2.10
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	220.441, 58.324, 151.410, 90.00, 114.25, 90.00
R / Rfree (%)	20.6 / 23.8

The binding sites of Calcium atom in the 4,6-Alpha-Glucanotransferase Gtfb From Lactobacillus Reuteri 121 Complexed with An Isomalto-Maltopentasaccharide (pdb code 5jbe). 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 From Lactobacillus Reuteri 121 Complexed with An Isomalto-Maltopentasaccharide, PDB code: 5jbe:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the 4,6-Alpha-Glucanotransferase Gtfb From Lactobacillus Reuteri 121 Complexed with An Isomalto-Maltopentasaccharide


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 From Lactobacillus Reuteri 121 Complexed with An Isomalto-Maltopentasaccharide within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1701 b:25.7 occ:1.00 OE2 A:GLU969 2.3 24.9 1.0 O A:GLU969 2.3 25.0 1.0 OD1 A:ASP975 2.4 25.1 1.0 OD1 A:ASN1483 2.4 24.5 1.0 O A:HOH1853 2.4 18.5 1.0 O A:ASN1019 2.5 28.4 1.0 OD2 A:ASP975 2.8 24.5 1.0 CG A:ASP975 2.9 25.1 1.0 CD A:GLU969 3.3 25.5 1.0 C A:GLU969 3.4 25.2 1.0 CG A:ASN1483 3.5 25.0 1.0 C A:ASN1019 3.7 28.4 1.0 CG A:GLU969 3.7 25.5 1.0 CA A:GLU969 4.0 25.3 1.0 ND2 A:ASN1483 4.1 25.0 1.0 O A:ASN1483 4.2 26.2 1.0 OE1 A:GLU969 4.4 25.5 1.0 O A:HOH1910 4.4 19.4 1.0 CG2 A:ILE1020 4.4 28.5 1.0 CB A:ASP975 4.4 25.6 1.0 CA A:ILE1020 4.4 28.2 1.0 CB A:GLU969 4.5 25.6 1.0 CB A:ASN1019 4.5 29.0 1.0 N A:ILE1020 4.5 28.3 1.0 N A:LEU970 4.5 25.4 1.0 O A:HOH1816 4.5 25.9 1.0 O A:ILE976 4.6 26.6 1.0 CB A:ASN1483 4.6 25.5 1.0 CA A:ASN1019 4.7 28.7 1.0 CA A:LEU970 4.8 25.9 1.0 CA A:ASN1483 4.8 25.8 1.0 ND2 A:ASN1574 4.8 26.2 1.0 C A:ASN1483 4.9 26.2 1.0 CD2 A:LEU970 5.0 26.6 1.0

Calcium binding site 2 out of 2 in the 4,6-Alpha-Glucanotransferase Gtfb From Lactobacillus Reuteri 121 Complexed with An Isomalto-Maltopentasaccharide


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 From Lactobacillus Reuteri 121 Complexed with An Isomalto-Maltopentasaccharide within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1701 b:32.7 occ:1.00 O B:HOH1997 2.2 35.5 1.0 O B:GLU969 2.3 34.5 1.0 OE2 B:GLU969 2.3 34.0 1.0 OD1 B:ASN1483 2.4 33.4 1.0 OD1 B:ASP975 2.4 33.9 1.0 O B:ASN1019 2.4 32.6 1.0 OD2 B:ASP975 2.8 33.7 1.0 CG B:ASP975 3.0 33.9 1.0 CD B:GLU969 3.3 34.7 1.0 C B:GLU969 3.4 34.7 1.0 CG B:ASN1483 3.5 33.7 1.0 C B:ASN1019 3.6 33.0 1.0 CG B:GLU969 3.7 34.9 1.0 CA B:GLU969 4.0 34.5 1.0 ND2 B:ASN1483 4.1 33.8 1.0 O B:ASN1483 4.2 34.1 1.0 O B:HOH1827 4.3 22.3 1.0 CG2 B:ILE1020 4.4 33.8 1.0 OE1 B:GLU969 4.4 34.5 1.0 CA B:ILE1020 4.4 33.7 1.0 CB B:ASN1019 4.4 32.5 1.0 N B:ILE1020 4.4 33.3 1.0 CB B:ASP975 4.5 34.3 1.0 CB B:GLU969 4.5 34.8 1.0 N B:LEU970 4.5 35.1 1.0 O B:HOH1832 4.5 30.0 1.0 CB B:ASN1483 4.6 33.6 1.0 O B:ILE976 4.6 34.3 1.0 CA B:ASN1019 4.6 32.5 1.0 CA B:ASN1483 4.7 33.9 1.0 CA B:LEU970 4.8 35.4 1.0 ND2 B:ASN1574 4.9 34.1 1.0 C B:ASN1483 4.9 34.4 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