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Calcium in PDB 3n9k: F229A/E292S Double Mutant of Exo-Beta-1,3-Glucanase From Candida Albicans in Complex with Laminaritriose at 1.7 A

Enzymatic activity of F229A/E292S Double Mutant of Exo-Beta-1,3-Glucanase From Candida Albicans in Complex with Laminaritriose at 1.7 A

All present enzymatic activity of F229A/E292S Double Mutant of Exo-Beta-1,3-Glucanase From Candida Albicans in Complex with Laminaritriose at 1.7 A:
3.2.1.58;

Protein crystallography data

The structure of F229A/E292S Double Mutant of Exo-Beta-1,3-Glucanase From Candida Albicans in Complex with Laminaritriose at 1.7 A, PDB code: 3n9k was solved by Y.Nakatani, S.M.Cutfield, J.F.Cutfield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.19 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.725, 64.397, 94.866, 90.00, 90.00, 90.00
R / Rfree (%) 15.2 / 19.7

Calcium Binding Sites:

The binding sites of Calcium atom in the F229A/E292S Double Mutant of Exo-Beta-1,3-Glucanase From Candida Albicans in Complex with Laminaritriose at 1.7 A (pdb code 3n9k). 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 F229A/E292S Double Mutant of Exo-Beta-1,3-Glucanase From Candida Albicans in Complex with Laminaritriose at 1.7 A, PDB code: 3n9k:

Calcium binding site 1 out of 1 in 3n9k

Go back to Calcium Binding Sites List in 3n9k
Calcium binding site 1 out of 1 in the F229A/E292S Double Mutant of Exo-Beta-1,3-Glucanase From Candida Albicans in Complex with Laminaritriose at 1.7 A


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of F229A/E292S Double Mutant of Exo-Beta-1,3-Glucanase From Candida Albicans in Complex with Laminaritriose at 1.7 A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1

b:16.1
occ:1.00
 O A:ARG265 2.2 14.2 1.0
O A:LEU263 2.3 14.9 1.0
O A:HOH439 2.3 13.4 1.0
O A:HOH440 2.4 15.6 1.0
O A:HOH407 2.5 16.5 1.0
NE2 A:HIS270 2.6 11.7 1.0
CD2 A:HIS270 3.4 12.2 1.0
C A:ARG265 3.4 14.8 1.0
C A:LEU263 3.5 13.6 1.0
CE1 A:HIS270 3.6 11.7 1.0
N A:ARG265 3.8 11.4 1.0
C A:SER264 4.0 13.2 1.0
CA A:ARG265 4.1 13.9 1.0
O A:SER264 4.4 12.9 1.0
CA A:LEU263 4.4 12.2 1.0
O A:HOH647 4.4 33.3 1.0
O A:HOH442 4.4 27.2 1.0
N A:SER264 4.5 14.4 1.0
N A:ASN266 4.5 12.1 1.0
O A:HOH441 4.5 28.8 1.0
CA A:SER264 4.5 14.8 1.0
CG A:HIS270 4.6 10.8 1.0
O A:LEU297 4.6 11.9 1.0
O A:HOH643 4.6 33.3 1.0
ND1 A:HIS270 4.7 11.8 1.0
CB A:ARG265 4.7 13.0 1.0
CA A:ASN266 4.7 14.3 1.0
O A:GLU262 4.7 12.1 1.0
C A:ASN266 4.8 15.2 1.0
O A:HOH443 4.9 20.7 1.0
O A:ASN266 5.0 16.1 1.0

Reference:

W.M.Patrick, Y.Nakatani, S.M.Cutfield, M.L.Sharpe, R.J.Ramsay, J.F.Cutfield. Carbohydrate Binding Sites in Candida Albicans Exo-Beta-1,3-Glucanase and the Role of the Phe-Phe 'Clamp' at the Active Site Entrance Febs J. V. 277 4549 2010.
ISSN: ISSN 1742-464X
PubMed: 20875088
DOI: 10.1111/J.1742-4658.2010.07869.X
Page generated: Sat Dec 12 04:21:51 2020

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