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Chlorine in PDB 3hl8: Crystal Structure of Exonuclease I in Complex with Inhibitor Bcbp
Enzymatic activity of Crystal Structure of Exonuclease I in Complex with Inhibitor Bcbp
All present enzymatic activity of Crystal Structure of Exonuclease I in Complex with Inhibitor Bcbp:
3.1.11.1;
3.1.11.1;
Protein crystallography data
The structure of Crystal Structure of Exonuclease I in Complex with Inhibitor Bcbp, PDB code: 3hl8
was solved by
K.A.Satyshur,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 26.91 / 1.55 |
| Space group | P 21 21 21 |
| Cell size a, b, c (Å), α, β, γ (°) | 53.823, 91.966, 106.280, 90.00, 90.00, 90.00 |
| R / Rfree (%) | 17.2 / 20.7 |
Other elements in 3hl8:
The structure of Crystal Structure of Exonuclease I in Complex with Inhibitor Bcbp also contains other interesting chemical elements:
| Magnesium | (Mg) | 1 atom |
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Exonuclease I in Complex with Inhibitor Bcbp
(pdb code 3hl8). 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 of Exonuclease I in Complex with Inhibitor Bcbp, PDB code: 3hl8:
In total only one binding site of Chlorine was determined in the Crystal Structure of Exonuclease I in Complex with Inhibitor Bcbp, PDB code: 3hl8:
Chlorine binding site 1 out of 1 in 3hl8
Go back to
Chlorine Binding Sites List in 3hl8
Chlorine binding site 1 out
of 1 in the Crystal Structure of Exonuclease I in Complex with Inhibitor Bcbp
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 of Exonuclease I in Complex with Inhibitor Bcbp within 5.0Å range:
|
Reference:
D.Lu,
D.A.Bernstein,
K.A.Satyshur,
J.L.Keck.
Small-Molecule Tools For Dissecting the Roles of Ssb/Protein Interactions in Genome Maintenance Proc.Natl.Acad.Sci.Usa V. 107 633 2010.
ISSN: ISSN 0027-8424
PubMed: 20018747
DOI: 10.1073/PNAS.0909191107
Page generated: Fri Jul 11 06:02:51 2025
ISSN: ISSN 0027-8424
PubMed: 20018747
DOI: 10.1073/PNAS.0909191107
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