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Atomistry » Calcium » PDB 1ex0-1fae » 1f9o » |
Calcium in PDB 1f9o: Crystal Structure of the Cellulase CEL48F From C. Cellulolyticum with the Thiooligosaccharide Inhibitor Pips-IG3Enzymatic activity of Crystal Structure of the Cellulase CEL48F From C. Cellulolyticum with the Thiooligosaccharide Inhibitor Pips-IG3
All present enzymatic activity of Crystal Structure of the Cellulase CEL48F From C. Cellulolyticum with the Thiooligosaccharide Inhibitor Pips-IG3:
3.2.1.4; Protein crystallography data
The structure of Crystal Structure of the Cellulase CEL48F From C. Cellulolyticum with the Thiooligosaccharide Inhibitor Pips-IG3, PDB code: 1f9o
was solved by
G.Parsiegla,
C.Reverbel-Leroy,
C.Tardif,
J.P.Belaich,
H.Driguez,
R.Haser,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1f9o:
The structure of Crystal Structure of the Cellulase CEL48F From C. Cellulolyticum with the Thiooligosaccharide Inhibitor Pips-IG3 also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of the Cellulase CEL48F From C. Cellulolyticum with the Thiooligosaccharide Inhibitor Pips-IG3
(pdb code 1f9o). 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 Cellulase CEL48F From C. Cellulolyticum with the Thiooligosaccharide Inhibitor Pips-IG3, PDB code: 1f9o: Calcium binding site 1 out of 1 in 1f9oGo back to Calcium Binding Sites List in 1f9o
Calcium binding site 1 out
of 1 in the Crystal Structure of the Cellulase CEL48F From C. Cellulolyticum with the Thiooligosaccharide Inhibitor Pips-IG3
Mono view Stereo pair view
Reference:
G.Parsiegla,
C.Reverbel-Leroy,
C.Tardif,
J.P.Belaich,
H.Driguez,
R.Haser.
Crystal Structures of the Cellulase CEL48F in Complex with Inhibitors and Substrates Give Insights Into Its Processive Action Biochemistry V. 39 11238 2000.
Page generated: Thu Jul 11 08:04:36 2024
ISSN: ISSN 0006-2960 PubMed: 10985769 DOI: 10.1021/BI001139P |
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