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Calcium in PDB 2qno: Crystal Structure of the Mutant E55Q of the Cellulase CEL48F in Complex with A Thio-Oligosaccharide

Enzymatic activity of Crystal Structure of the Mutant E55Q of the Cellulase CEL48F in Complex with A Thio-Oligosaccharide

All present enzymatic activity of Crystal Structure of the Mutant E55Q of the Cellulase CEL48F in Complex with A Thio-Oligosaccharide:
3.2.1.4;

Protein crystallography data

The structure of Crystal Structure of the Mutant E55Q of the Cellulase CEL48F in Complex with A Thio-Oligosaccharide, PDB code: 2qno was solved by G.Parsiegla, R.Haser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.30 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 61.240, 84.720, 121.740, 90.00, 90.00, 90.00
R / Rfree (%) 13.7 / 18.2

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Mutant E55Q of the Cellulase CEL48F in Complex with A Thio-Oligosaccharide (pdb code 2qno). 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 the Mutant E55Q of the Cellulase CEL48F in Complex with A Thio-Oligosaccharide, PDB code: 2qno:

Calcium binding site 1 out of 1 in 2qno

Go back to Calcium Binding Sites List in 2qno
Calcium binding site 1 out of 1 in the Crystal Structure of the Mutant E55Q of the Cellulase CEL48F in Complex with A Thio-Oligosaccharide


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 the Mutant E55Q of the Cellulase CEL48F in Complex with A Thio-Oligosaccharide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca2000

b:17.5
occ:1.00
 OD2 A:ASP405 2.3 15.8 1.0
O A:GLN185 2.3 12.8 1.0
OE2 A:GLU190 2.4 13.9 1.0
O A:HOH2162 2.4 18.1 1.0
O A:HOH2136 2.4 18.6 1.0
OE1 A:GLN185 2.6 20.8 1.0
OE1 A:GLU190 2.6 15.7 1.0
CD A:GLU190 2.8 12.4 1.0
CG A:ASP405 3.5 17.8 1.0
C A:GLN185 3.5 13.6 1.0
CD A:GLN185 3.8 21.0 1.0
CB A:ASP405 4.0 16.6 1.0
CB A:GLN185 4.1 15.3 1.0
CA A:GLN185 4.2 15.0 1.0
NH2 A:ARG549 4.2 20.1 1.0
O A:HOH2433 4.3 36.7 1.0
N A:SER187 4.3 11.6 1.0
CG A:GLU190 4.3 9.1 1.0
O A:HOH2293 4.5 45.4 1.0
OD1 A:ASP405 4.5 17.5 1.0
CG A:GLN185 4.5 18.6 1.0
N A:GLU186 4.6 13.5 1.0
OG A:SER187 4.7 10.1 1.0
CA A:GLU186 4.8 11.7 1.0
CB A:SER187 4.8 10.8 1.0
NE2 A:GLN185 4.8 20.8 1.0
O A:HOH2394 4.9 46.8 1.0
O A:HOH2164 4.9 23.6 1.0

Reference:

G.Parsiegla, C.Reverbel, C.Tardif, H.Driguez, R.Haser. Structures of Mutants of Cellulase CEL48F of Clostridium Cellulolyticum in Complex with Long Hemithiocellooligosaccharides Give Rise to A New View of the Substrate Pathway During Processive Action J.Mol.Biol. V. 375 499 2008.
ISSN: ISSN 0022-2836
PubMed: 18035374
DOI: 10.1016/J.JMB.2007.10.039
Page generated: Tue Jul 8 07:54:55 2025

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