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Chlorine in PDB 3qng: Crystal Structure Analysis of Lysozyme-Bound Fac-[Re(Co)3(L-Serine)]
Enzymatic activity of Crystal Structure Analysis of Lysozyme-Bound Fac-[Re(Co)3(L-Serine)]
All present enzymatic activity of Crystal Structure Analysis of Lysozyme-Bound Fac-[Re(Co)3(L-Serine)]:
3.2.1.17;
3.2.1.17;
Protein crystallography data
The structure of Crystal Structure Analysis of Lysozyme-Bound Fac-[Re(Co)3(L-Serine)], PDB code: 3qng
was solved by
F.Zobi,
B.Spingler,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 33.12 / 1.55 |
| Space group | P 43 21 2 |
| Cell size a, b, c (Å), α, β, γ (°) | 78.343, 78.343, 36.546, 90.00, 90.00, 90.00 |
| R / Rfree (%) | 18.5 / 21.7 |
Other elements in 3qng:
The structure of Crystal Structure Analysis of Lysozyme-Bound Fac-[Re(Co)3(L-Serine)] also contains other interesting chemical elements:
| Rhenium | (Re) | 1 atom |
| Sodium | (Na) | 1 atom |
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure Analysis of Lysozyme-Bound Fac-[Re(Co)3(L-Serine)]
(pdb code 3qng). 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 Crystal Structure Analysis of Lysozyme-Bound Fac-[Re(Co)3(L-Serine)], PDB code: 3qng:
In total only one binding site of Chlorine was determined in the Crystal Structure Analysis of Lysozyme-Bound Fac-[Re(Co)3(L-Serine)], PDB code: 3qng:
Chlorine binding site 1 out of 1 in 3qng
Go back to
Chlorine Binding Sites List in 3qng
Chlorine binding site 1 out
of 1 in the Crystal Structure Analysis of Lysozyme-Bound Fac-[Re(Co)3(L-Serine)]
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Chlorine with other atoms in the Cl binding
site number 1 of Crystal Structure Analysis of Lysozyme-Bound Fac-[Re(Co)3(L-Serine)] within 5.0Å range:
|
Reference:
F.Zobi,
B.Spingler.
Post-Protein-Binding Reactivity and Modifications of the Fac-[Re(Co)3]+ Core Inorg.Chem. V. 51 1210 2012.
ISSN: ISSN 0020-1669
PubMed: 22229733
DOI: 10.1021/IC2023314
Page generated: Fri Jul 11 09:27:36 2025
ISSN: ISSN 0020-1669
PubMed: 22229733
DOI: 10.1021/IC2023314
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