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Thallium in PDB 2bob: Potassium Channel Kcsa-Fab Complex in Thallium with Tetrabutylammonium (Tba)

Protein crystallography data

The structure of Potassium Channel Kcsa-Fab Complex in Thallium with Tetrabutylammonium (Tba), PDB code: 2bob was solved by M.J.Lenaeus, M.Vamvouka, P.J.Focia, A.Gross, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.76
Space group I 4
Cell size a, b, c (Å), α, β, γ (°) 155.267, 155.267, 75.555, 90.00, 90.00, 90.00
R / Rfree (%) 22 / 25.1

Other elements in 2bob:

The structure of Potassium Channel Kcsa-Fab Complex in Thallium with Tetrabutylammonium (Tba) also contains other interesting chemical elements:

Cobalt (Co) 1 atom

Thallium Binding Sites:

The binding sites of Thallium atom in the Potassium Channel Kcsa-Fab Complex in Thallium with Tetrabutylammonium (Tba) (pdb code 2bob). This binding sites where shown within 5.0 Angstroms radius around Thallium atom.
In total only one binding site of Thallium was determined in the Potassium Channel Kcsa-Fab Complex in Thallium with Tetrabutylammonium (Tba), PDB code: 2bob:

Thallium binding site 1 out of 1 in 2bob

Go back to Thallium Binding Sites List in 2bob
Thallium binding site 1 out of 1 in the Potassium Channel Kcsa-Fab Complex in Thallium with Tetrabutylammonium (Tba)


Mono view


Stereo pair view

A full contact list of Thallium with other atoms in the Tl binding site number 1 of Potassium Channel Kcsa-Fab Complex in Thallium with Tetrabutylammonium (Tba) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Tl201

b:31.9
occ:0.25
O C:THR75 3.0 21.0 1.0
OG1 C:THR75 3.2 21.0 1.0
CB C:THR75 3.6 21.1 1.0
C C:THR75 4.1 21.0 1.0
C31 C:TBA203 4.3 21.1 0.1
C41 C:TBA203 4.4 20.8 0.1
C11 C:TBA203 4.4 21.1 0.1
CA C:THR75 4.5 21.1 1.0
C21 C:TBA203 4.6 20.8 0.1
CG2 C:THR75 4.7 21.1 1.0

Reference:

M.J.Lenaeus, M.Vamvouka, P.J.Focia, A.Gross. Structural Basis of Tea Blockade in A Model Potassium Channel Nat.Struct.Mol.Biol. V. 12 454 2005.
ISSN: ISSN 1545-9993
PubMed: 15852022
DOI: 10.1038/NSMB929
Page generated: Wed Dec 16 02:28:38 2020

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