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Atomistry » Potassium » PDB 4cn5-4edj » 4doo | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Potassium » PDB 4cn5-4edj » 4doo » |
Potassium in PDB 4doo: Crystal Structure of Arabidopsis Thaliana Fatty-Acid Binding Protein AT3G63170 (ATFAP1)Protein crystallography data
The structure of Crystal Structure of Arabidopsis Thaliana Fatty-Acid Binding Protein AT3G63170 (ATFAP1), PDB code: 4doo
was solved by
J.P.Noel,
F.Pojer,
G.V.Louie,
M.E.Bowman,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Potassium Binding Sites:
The binding sites of Potassium atom in the Crystal Structure of Arabidopsis Thaliana Fatty-Acid Binding Protein AT3G63170 (ATFAP1)
(pdb code 4doo). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of Arabidopsis Thaliana Fatty-Acid Binding Protein AT3G63170 (ATFAP1), PDB code: 4doo: Jump to Potassium binding site number: 1; 2; Potassium binding site 1 out of 2 in 4dooGo back to Potassium Binding Sites List in 4doo
Potassium binding site 1 out
of 2 in the Crystal Structure of Arabidopsis Thaliana Fatty-Acid Binding Protein AT3G63170 (ATFAP1)
Mono view Stereo pair view
Potassium binding site 2 out of 2 in 4dooGo back to Potassium Binding Sites List in 4doo
Potassium binding site 2 out
of 2 in the Crystal Structure of Arabidopsis Thaliana Fatty-Acid Binding Protein AT3G63170 (ATFAP1)
Mono view Stereo pair view
Reference:
M.N.Ngaki,
G.V.Louie,
R.N.Philippe,
G.Manning,
F.Pojer,
M.E.Bowman,
L.Li,
E.Larsen,
E.S.Wurtele,
J.P.Noel.
Evolution of the Chalcone-Isomerase Fold From Fatty-Acid Binding to Stereospecific Catalysis. Nature V. 485 530 2012.
Page generated: Sun Dec 13 23:30:06 2020
ISSN: ISSN 0028-0836 PubMed: 22622584 DOI: 10.1038/NATURE11009 |
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