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Atomistry » Chlorine » PDB 3lcc-3lnj » 3lf1 » |
Chlorine in PDB 3lf1: Apo Structure of the Short Chain Oxidoreductase Q9HYA2 From Pseudomonas Aeruginosa PAO1 Containing An Atypical Catalytic CenterProtein crystallography data
The structure of Apo Structure of the Short Chain Oxidoreductase Q9HYA2 From Pseudomonas Aeruginosa PAO1 Containing An Atypical Catalytic Center, PDB code: 3lf1
was solved by
R.Huether,
T.C.Umland,
W.L.Duax,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3lf1:
The structure of Apo Structure of the Short Chain Oxidoreductase Q9HYA2 From Pseudomonas Aeruginosa PAO1 Containing An Atypical Catalytic Center also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Apo Structure of the Short Chain Oxidoreductase Q9HYA2 From Pseudomonas Aeruginosa PAO1 Containing An Atypical Catalytic Center
(pdb code 3lf1). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Apo Structure of the Short Chain Oxidoreductase Q9HYA2 From Pseudomonas Aeruginosa PAO1 Containing An Atypical Catalytic Center, PDB code: 3lf1: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 3lf1Go back to Chlorine Binding Sites List in 3lf1
Chlorine binding site 1 out
of 2 in the Apo Structure of the Short Chain Oxidoreductase Q9HYA2 From Pseudomonas Aeruginosa PAO1 Containing An Atypical Catalytic Center
Mono view Stereo pair view
Chlorine binding site 2 out of 2 in 3lf1Go back to Chlorine Binding Sites List in 3lf1
Chlorine binding site 2 out
of 2 in the Apo Structure of the Short Chain Oxidoreductase Q9HYA2 From Pseudomonas Aeruginosa PAO1 Containing An Atypical Catalytic Center
Mono view Stereo pair view
Reference:
R.Huether,
Q.Mao,
W.L.Duax,
T.C.Umland.
The Short-Chain Oxidoreductase Q9HYA2 From Pseudomonas Aeruginosa PAO1 Contains An Atypical Catalytic Center. Protein Sci. V. 19 1097 2010.
Page generated: Sat Dec 12 09:53:03 2020
ISSN: ISSN 0961-8368 PubMed: 20340135 DOI: 10.1002/PRO.384 |
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