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Atomistry » Aluminium » PDB 1a6e-1tx4 » 1he1 » |
Aluminium in PDB 1he1: Crystal Structure of the Complex Between the Gap Domain of the Pseudomonas Aeruginosa Exos Toxin and Human RacProtein crystallography data
The structure of Crystal Structure of the Complex Between the Gap Domain of the Pseudomonas Aeruginosa Exos Toxin and Human Rac, PDB code: 1he1
was solved by
M.Wurtele,
E.Wolf,
K.J.Pederson,
G.Buchwald,
M.R.Ahmadian,
J.T.Barbieri,
A.Wittinghofer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1he1:
The structure of Crystal Structure of the Complex Between the Gap Domain of the Pseudomonas Aeruginosa Exos Toxin and Human Rac also contains other interesting chemical elements:
Aluminium Binding Sites:
The binding sites of Aluminium atom in the Crystal Structure of the Complex Between the Gap Domain of the Pseudomonas Aeruginosa Exos Toxin and Human Rac
(pdb code 1he1). This binding sites where shown within
5.0 Angstroms radius around Aluminium atom.
In total 2 binding sites of Aluminium where determined in the Crystal Structure of the Complex Between the Gap Domain of the Pseudomonas Aeruginosa Exos Toxin and Human Rac, PDB code: 1he1: Jump to Aluminium binding site number: 1; 2; Aluminium binding site 1 out of 2 in 1he1Go back to![]() ![]()
Aluminium binding site 1 out
of 2 in the Crystal Structure of the Complex Between the Gap Domain of the Pseudomonas Aeruginosa Exos Toxin and Human Rac
![]() Mono view ![]() Stereo pair view
Aluminium binding site 2 out of 2 in 1he1Go back to![]() ![]()
Aluminium binding site 2 out
of 2 in the Crystal Structure of the Complex Between the Gap Domain of the Pseudomonas Aeruginosa Exos Toxin and Human Rac
![]() Mono view ![]() Stereo pair view
Reference:
M.Wurtele,
E.Wolf,
K.J.Pederson,
G.Buchwald,
M.R.Ahmadian,
J.T.Barbieri,
A.Wittinghofer.
How the Pseudomonas Aeruginosa Exos Toxin Downregulates Rac Nat.Struct.Biol. V. 8 23 2001.
Page generated: Sat Dec 12 01:30:12 2020
ISSN: ISSN 1072-8368 PubMed: 11135665 DOI: 10.1038/83007 |
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