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Atomistry » Chlorine » PDB 3ck2-3csw » 3cl9 » |
Chlorine in PDB 3cl9: Structure of Bifunctional Tcdhfr-Ts in Complex with MtxEnzymatic activity of Structure of Bifunctional Tcdhfr-Ts in Complex with Mtx
All present enzymatic activity of Structure of Bifunctional Tcdhfr-Ts in Complex with Mtx:
1.5.1.3; 2.1.1.45; Protein crystallography data
The structure of Structure of Bifunctional Tcdhfr-Ts in Complex with Mtx, PDB code: 3cl9
was solved by
N.Schormann,
O.Senkovich,
D.Chattopadhyay,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Structure of Bifunctional Tcdhfr-Ts in Complex with Mtx
(pdb code 3cl9). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Structure of Bifunctional Tcdhfr-Ts in Complex with Mtx, PDB code: 3cl9: Jump to Chlorine binding site number: 1; 2; 3; Chlorine binding site 1 out of 3 in 3cl9Go back to![]() ![]()
Chlorine binding site 1 out
of 3 in the Structure of Bifunctional Tcdhfr-Ts in Complex with Mtx
![]() Mono view ![]() Stereo pair view
Chlorine binding site 2 out of 3 in 3cl9Go back to![]() ![]()
Chlorine binding site 2 out
of 3 in the Structure of Bifunctional Tcdhfr-Ts in Complex with Mtx
![]() Mono view ![]() Stereo pair view
Chlorine binding site 3 out of 3 in 3cl9Go back to![]() ![]()
Chlorine binding site 3 out
of 3 in the Structure of Bifunctional Tcdhfr-Ts in Complex with Mtx
![]() Mono view ![]() Stereo pair view
Reference:
N.Schormann,
O.Senkovich,
K.Walker,
D.L.Wright,
A.C.Anderson,
A.Rosowsky,
S.Ananthan,
B.Shinkre,
S.Velu,
D.Chattopadhyay.
Structure-Based Approach to Pharmacophore Identification, in Silico Screening, and Three-Dimensional Quantitative Structure-Activity Relationship Studies For Inhibitors of Trypanosoma Cruzi Dihydrofolate Reductase Function. Proteins V. 73 889 2008.
Page generated: Fri Jul 11 04:05:50 2025
ISSN: ISSN 0887-3585 PubMed: 18536013 DOI: 10.1002/PROT.22115 |
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