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Calcium in PDB 3kll: Crystal Structure of Lactobacillus Reuteri N-Terminally Truncated Glucansucrase GTF180-Maltose Complex

Enzymatic activity of Crystal Structure of Lactobacillus Reuteri N-Terminally Truncated Glucansucrase GTF180-Maltose Complex

All present enzymatic activity of Crystal Structure of Lactobacillus Reuteri N-Terminally Truncated Glucansucrase GTF180-Maltose Complex:
2.4.1.5;

Protein crystallography data

The structure of Crystal Structure of Lactobacillus Reuteri N-Terminally Truncated Glucansucrase GTF180-Maltose Complex, PDB code: 3kll was solved by A.Vujicic-Zagar, T.Pijning, S.Kralj, W.Eeuwema, L.Dijkhuizen, B.W.Dijkstra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 58.165, 65.850, 82.317, 73.44, 78.57, 86.34
R / Rfree (%) 16.3 / 19.9

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Lactobacillus Reuteri N-Terminally Truncated Glucansucrase GTF180-Maltose Complex (pdb code 3kll). 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 Crystal Structure of Lactobacillus Reuteri N-Terminally Truncated Glucansucrase GTF180-Maltose Complex, PDB code: 3kll:

Calcium binding site 1 out of 1 in 3kll

Go back to Calcium Binding Sites List in 3kll
Calcium binding site 1 out of 1 in the Crystal Structure of Lactobacillus Reuteri N-Terminally Truncated Glucansucrase GTF180-Maltose Complex


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Lactobacillus Reuteri N-Terminally Truncated Glucansucrase GTF180-Maltose Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1

b:20.1
occ:1.00
 O A:ASN1029 2.2 21.5 1.0
O A:GLU979 2.2 19.8 1.0
OD1 A:ASP985 2.4 16.6 1.0
OE2 A:GLU979 2.5 17.3 1.0
O A:HOH436 2.5 20.8 1.0
OD1 A:ASP1508 2.6 15.4 1.0
OD2 A:ASP985 2.6 18.0 1.0
CG A:ASP985 2.9 19.5 1.0
C A:GLU979 3.4 20.5 1.0
CD A:GLU979 3.4 24.6 1.0
C A:ASN1029 3.5 21.2 1.0
CG A:ASP1508 3.7 20.9 1.0
CG A:GLU979 3.7 20.4 1.0
CA A:GLU979 4.0 20.2 1.0
OD2 A:ASP1508 4.3 18.1 1.0
O A:ASP1508 4.3 18.6 1.0
N A:VAL1030 4.3 20.3 1.0
CA A:VAL1030 4.3 19.6 1.0
CB A:ASP985 4.3 18.6 1.0
CB A:ASN1029 4.4 20.6 1.0
CG1 A:VAL1030 4.4 19.0 1.0
O A:ILE986 4.4 17.1 1.0
O A:HOH14 4.4 18.9 1.0
CA A:ASN1029 4.4 21.3 1.0
N A:PHE980 4.5 20.4 1.0
CB A:GLU979 4.5 20.7 1.0
OE1 A:GLU979 4.5 18.3 1.0
ND2 A:ASN1597 4.6 18.7 1.0
O A:HOH433 4.7 20.7 1.0
CB A:ASP1508 4.8 17.1 1.0
CA A:PHE980 4.8 21.3 1.0
CA A:ASP1508 4.9 18.4 1.0
CB A:VAL1030 5.0 20.9 1.0

Reference:

A.Vujicic-Zagar, T.Pijning, S.Kralj, C.A.Lopez, W.Eeuwema, L.Dijkhuizen, B.W.Dijkstra. Crystal Structure of A 117 kDa Glucansucrase Fragment Provides Insight Into Evolution and Product Specificity of GH70 Enzymes Proc.Natl.Acad.Sci.Usa V. 107 21406 2010.
ISSN: ISSN 0027-8424
PubMed: 21118988
DOI: 10.1073/PNAS.1007531107
Page generated: Sat Dec 12 04:17:41 2020

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