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Chlorine in PDB 1g9j: X-Tal Structure of the Mutant E44Q of the Cellulase CEL48F in Complex with A Thiooligosaccharide

Enzymatic activity of X-Tal Structure of the Mutant E44Q of the Cellulase CEL48F in Complex with A Thiooligosaccharide

All present enzymatic activity of X-Tal Structure of the Mutant E44Q of the Cellulase CEL48F in Complex with A Thiooligosaccharide:
3.2.1.4;

Protein crystallography data

The structure of X-Tal Structure of the Mutant E44Q of the Cellulase CEL48F in Complex with A Thiooligosaccharide, PDB code: 1g9j was solved by G.Parsiegla, C.Tardif, J.P.Belaich, H.Driguez, R.Haser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.76 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 61.480, 84.720, 121.810, 90.00, 90.00, 90.00
R / Rfree (%) 18.2 / 20.7

Other elements in 1g9j:

The structure of X-Tal Structure of the Mutant E44Q of the Cellulase CEL48F in Complex with A Thiooligosaccharide also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the X-Tal Structure of the Mutant E44Q of the Cellulase CEL48F in Complex with A Thiooligosaccharide (pdb code 1g9j). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the X-Tal Structure of the Mutant E44Q of the Cellulase CEL48F in Complex with A Thiooligosaccharide, PDB code: 1g9j:

Chlorine binding site 1 out of 1 in 1g9j

Go back to Chlorine Binding Sites List in 1g9j
Chlorine binding site 1 out of 1 in the X-Tal Structure of the Mutant E44Q of the Cellulase CEL48F in Complex with A Thiooligosaccharide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of X-Tal Structure of the Mutant E44Q of the Cellulase CEL48F in Complex with A Thiooligosaccharide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1385

b:29.2
occ:1.00
 O A:HOH1491 3.0 31.6 1.0
NE A:ARG609 3.1 16.0 1.0
CG A:GLN44 3.3 20.0 0.5
NE2 A:HIS36 3.3 13.0 1.0
CD A:ARG609 3.4 15.1 1.0
NE1 A:TRP611 3.6 14.3 1.0
CE1 A:HIS36 3.6 12.4 1.0
CG A:GLN44 3.6 19.9 0.5
CD A:GLN44 3.7 20.6 0.5
CB A:GLN44 3.8 19.0 0.5
OE1 A:GLN44 3.9 20.6 0.5
CB A:GLN44 3.9 18.9 0.5
O A:HOH1759 4.0 19.3 0.5
CZ A:ARG609 4.3 16.7 1.0
CG A:ARG609 4.3 14.3 1.0
OE1 A:GLN44 4.4 20.4 0.5
CD A:GLN44 4.5 20.4 0.5
CD1 A:TRP611 4.5 13.9 1.0
CE2 A:TRP611 4.5 14.1 1.0
NE2 A:GLN44 4.6 20.9 0.5
NH2 A:ARG609 4.6 17.1 1.0
CD2 A:HIS36 4.6 11.8 1.0
CZ2 A:TRP611 4.8 14.4 1.0
ND1 A:HIS36 4.9 11.7 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: Fri Jul 19 22:09:46 2024

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