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Calcium in PDB 1gbg: Bacillus Licheniformis Beta-Glucanase

Enzymatic activity of Bacillus Licheniformis Beta-Glucanase

All present enzymatic activity of Bacillus Licheniformis Beta-Glucanase:
3.2.1.73;

Protein crystallography data

The structure of Bacillus Licheniformis Beta-Glucanase, PDB code: 1gbg was solved by M.Hahn, U.Heinemann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 1.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 35.330, 39.130, 43.880, 64.66, 105.86, 110.68
R / Rfree (%) n/a / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the Bacillus Licheniformis Beta-Glucanase (pdb code 1gbg). 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 Bacillus Licheniformis Beta-Glucanase, PDB code: 1gbg:

Calcium binding site 1 out of 1 in 1gbg

Go back to Calcium Binding Sites List in 1gbg
Calcium binding site 1 out of 1 in the Bacillus Licheniformis Beta-Glucanase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Bacillus Licheniformis Beta-Glucanase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca373

b:28.1
occ:1.00
O A:GLY45 2.6 23.3 1.0
O A:PRO9 2.6 24.1 1.0
O A:HOH287 2.6 39.3 1.0
O A:ASN207 2.7 20.9 1.0
OD1 A:ASN207 2.7 22.4 1.0
O A:HOH289 2.8 42.5 1.0
C A:ASN207 3.7 23.2 1.0
C A:PRO9 3.7 19.5 1.0
CG A:ASN207 3.7 21.9 1.0
C A:GLY45 3.7 27.9 1.0
CA A:ASN207 4.2 20.9 1.0
CA A:PRO9 4.4 19.7 1.0
CA A:GLY45 4.5 28.0 1.0
O A:HOH370 4.5 54.7 1.0
CB A:PHE10 4.5 21.3 1.0
ND2 A:ASN207 4.6 23.7 1.0
CB A:ASN207 4.6 21.3 1.0
O A:PHE10 4.6 24.8 1.0
N A:PHE10 4.7 20.6 1.0
N A:TRP208 4.8 17.8 1.0
N A:GLU46 4.8 26.3 1.0
O A:LEU44 4.8 32.8 1.0
CB A:TRP208 4.8 16.0 1.0
CB A:PRO9 4.9 20.9 1.0
C A:PHE10 4.9 26.1 1.0
CA A:PHE10 4.9 23.9 1.0
CA A:GLU46 4.9 24.3 1.0

Reference:

M.Hahn, J.Pons, A.Planas, E.Querol, U.Heinemann. Crystal Structure of Bacillus Licheniformis 1,3-1,4-Beta-D-Glucan 4-Glucanohydrolase at 1.8 A Resolution. Febs Lett. V. 374 221 1995.
ISSN: ISSN 0014-5793
PubMed: 7589539
DOI: 10.1016/0014-5793(95)01111-Q
Page generated: Mon Jul 7 15:13:00 2025

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