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Calcium in PDB 3zqx: Carbohydrate-Binding Module CBM3B From the Cellulosomal Cellobiohydrolase 9A From Clostridium Thermocellum

Enzymatic activity of Carbohydrate-Binding Module CBM3B From the Cellulosomal Cellobiohydrolase 9A From Clostridium Thermocellum

All present enzymatic activity of Carbohydrate-Binding Module CBM3B From the Cellulosomal Cellobiohydrolase 9A From Clostridium Thermocellum:
3.2.1.91;

Protein crystallography data

The structure of Carbohydrate-Binding Module CBM3B From the Cellulosomal Cellobiohydrolase 9A From Clostridium Thermocellum, PDB code: 3zqx was solved by O.Yaniv, S.Petkun, L.J.W.Shimon, E.A.Bayer, R.Lamed, F.Frolow, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.33 / 1.04
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 50.036, 50.036, 122.595, 90.00, 90.00, 90.00
R / Rfree (%) 16.7 / 17.1

Calcium Binding Sites:

The binding sites of Calcium atom in the Carbohydrate-Binding Module CBM3B From the Cellulosomal Cellobiohydrolase 9A From Clostridium Thermocellum (pdb code 3zqx). 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 Carbohydrate-Binding Module CBM3B From the Cellulosomal Cellobiohydrolase 9A From Clostridium Thermocellum, PDB code: 3zqx:

Calcium binding site 1 out of 1 in 3zqx

Go back to Calcium Binding Sites List in 3zqx
Calcium binding site 1 out of 1 in the Carbohydrate-Binding Module CBM3B From the Cellulosomal Cellobiohydrolase 9A From Clostridium Thermocellum


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Carbohydrate-Binding Module CBM3B From the Cellulosomal Cellobiohydrolase 9A From Clostridium Thermocellum within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1146

b:8.8
occ:1.00
 OD1 A:ASP113 2.4 8.5 1.0
O A:ASP109 2.4 9.5 1.0
O A:THR44 2.4 9.4 1.0
OD1 A:ASN112 2.4 10.0 1.0
O A:HOH2100 2.5 9.6 1.0
OE2 A:GLU46 2.5 10.8 1.0
OE1 A:GLU46 2.5 9.9 1.0
OG1 A:THR44 2.6 9.8 1.0
CD A:GLU46 2.9 10.1 1.0
CG A:ASP113 3.4 7.9 1.0
C A:THR44 3.4 8.5 1.0
CG A:ASN112 3.4 10.8 1.0
C A:ASP109 3.6 9.0 1.0
CB A:THR44 3.7 9.4 1.0
OD2 A:ASP113 3.7 8.6 1.0
N A:THR44 3.8 8.4 1.0
CA A:THR44 3.8 9.3 1.0
ND2 A:ASN112 3.9 13.5 1.0
N A:ASP109 4.2 9.4 1.0
O A:HOH2099 4.3 11.8 1.0
CA A:ASP109 4.3 9.4 1.0
O A:ASN112 4.4 10.4 1.0
C A:ASN112 4.4 9.4 1.0
CG A:GLU46 4.4 12.2 1.0
CB A:ASP109 4.4 11.7 1.0
N A:GLN110 4.6 9.3 1.0
N A:LYS45 4.6 9.3 1.0
N A:ASP113 4.6 8.8 1.0
CA A:GLN110 4.7 9.5 1.0
CB A:ASN112 4.7 12.1 1.0
CB A:ASP113 4.7 8.5 1.0
O A:HOH2103 4.8 19.4 1.0
N A:ASN112 4.8 10.0 1.0
CA A:ASN112 4.9 10.4 1.0
CA A:ASP113 4.9 8.4 1.0
C A:PHE43 4.9 7.4 1.0
CG2 A:THR44 4.9 10.6 1.0
N A:GLU46 5.0 11.3 1.0
CA A:LYS45 5.0 9.9 1.0

Reference:

O.Yaniv, S.Petkun, L.J.W.Shimon, E.A.Bayer, R.Lamed, F.Frolow. A Single Mutation Reforms the Binding Activity of An Adhesion-Deficient Family 3 Carbohydrate-Binding Module Acta Crystallogr.,Sect.D V. 68 819 2012.
ISSN: ISSN 0907-4449
PubMed: 22751667
DOI: 10.1107/S0907444912013133
Page generated: Sat Dec 12 04:37:31 2020

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