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Atomistry » Chlorine » PDB 5esg-5f00 » 5esr | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 5esg-5f00 » 5esr » |
Chlorine in PDB 5esr: Crystal Structure of Haloalkane Dehalogenase (Dcca) From Caulobacter CrescentusEnzymatic activity of Crystal Structure of Haloalkane Dehalogenase (Dcca) From Caulobacter Crescentus
All present enzymatic activity of Crystal Structure of Haloalkane Dehalogenase (Dcca) From Caulobacter Crescentus:
3.8.1.5; Protein crystallography data
The structure of Crystal Structure of Haloalkane Dehalogenase (Dcca) From Caulobacter Crescentus, PDB code: 5esr
was solved by
V.N.Malashkevich,
R.Toro,
E.C.Mundorff,
S.C.Almo,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5esr:
The structure of Crystal Structure of Haloalkane Dehalogenase (Dcca) From Caulobacter Crescentus also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Haloalkane Dehalogenase (Dcca) From Caulobacter Crescentus
(pdb code 5esr). 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 Haloalkane Dehalogenase (Dcca) From Caulobacter Crescentus, PDB code: 5esr: Chlorine binding site 1 out of 1 in 5esrGo back to Chlorine Binding Sites List in 5esr
Chlorine binding site 1 out
of 1 in the Crystal Structure of Haloalkane Dehalogenase (Dcca) From Caulobacter Crescentus
Mono view Stereo pair view
Reference:
L.Carlucci,
E.Zhou,
V.N.Malashkevich,
S.C.Almo,
E.C.Mundorff.
Biochemical Characterization of Two Haloalkane Dehalogenases: Dcca From Caulobacter Crescentus and Dsaa From Saccharomonospora Azurea. Protein Sci. V. 25 877 2016.
Page generated: Sat Dec 12 11:42:02 2020
ISSN: ESSN 1469-896X PubMed: 26833751 DOI: 10.1002/PRO.2895 |
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