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Atomistry » Chlorine » PDB 2r74-2rg9 » 2rg1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 2r74-2rg9 » 2rg1 » |
Chlorine in PDB 2rg1: Crystal Structure of E. Coli Wrba ApoproteinEnzymatic activity of Crystal Structure of E. Coli Wrba Apoprotein
All present enzymatic activity of Crystal Structure of E. Coli Wrba Apoprotein:
1.6.5.2; Protein crystallography data
The structure of Crystal Structure of E. Coli Wrba Apoprotein, PDB code: 2rg1
was solved by
I.Kuta Smatanova,
J.Wolfova,
J.Brynda,
M.Lapkouski,
J.R.Mesters,
R.Grandori,
J.Carey,
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 Crystal Structure of E. Coli Wrba Apoprotein
(pdb code 2rg1). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of E. Coli Wrba Apoprotein, PDB code: 2rg1: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 2rg1Go back to Chlorine Binding Sites List in 2rg1
Chlorine binding site 1 out
of 2 in the Crystal Structure of E. Coli Wrba Apoprotein
Mono view Stereo pair view
Chlorine binding site 2 out of 2 in 2rg1Go back to Chlorine Binding Sites List in 2rg1
Chlorine binding site 2 out
of 2 in the Crystal Structure of E. Coli Wrba Apoprotein
Mono view Stereo pair view
Reference:
J.Wolfova,
I.K.Smatanova,
J.Brynda,
J.R.Mesters,
M.Lapkouski,
M.Kuty,
A.Natalello,
N.Chatterjee,
S.Y.Chern,
E.Ebbel,
A.Ricci,
R.Grandori,
R.Ettrich,
J.Carey.
Structural Organization of Wrba in Apo- and Holoprotein Crystals. Biochim.Biophys.Acta V.1794 1288 2009.
Page generated: Sat Dec 12 09:18:46 2020
ISSN: ISSN 0006-3002 PubMed: 19665595 DOI: 10.1016/J.BBAPAP.2009.08.001 |
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