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Potassium in PDB 4c0o: Transportin 3 in Complex with Phosphorylated Asf/SF2

Protein crystallography data

The structure of Transportin 3 in Complex with Phosphorylated Asf/SF2, PDB code: 4c0o was solved by G.N.Maertens, N.J.Cook, P.Cherepanov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.283 / 2.56
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 80.552, 91.062, 98.122, 106.98, 100.30, 102.18
R / Rfree (%) 22.12 / 26.91

Potassium Binding Sites:

The binding sites of Potassium atom in the Transportin 3 in Complex with Phosphorylated Asf/SF2 (pdb code 4c0o). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Transportin 3 in Complex with Phosphorylated Asf/SF2, PDB code: 4c0o:

Potassium binding site 1 out of 1 in 4c0o

Go back to Potassium Binding Sites List in 4c0o
Potassium binding site 1 out of 1 in the Transportin 3 in Complex with Phosphorylated Asf/SF2


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Transportin 3 in Complex with Phosphorylated Asf/SF2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K1924

b:70.5
occ:1.00
ND1 B:HIS745 2.9 44.3 1.0
OD1 B:ASP747 3.0 37.0 1.0
OD2 B:ASP747 3.3 43.9 1.0
OG1 B:THR748 3.4 38.9 1.0
CG B:ASP747 3.5 35.4 1.0
CB B:HIS745 3.5 33.1 1.0
CG B:HIS745 3.6 47.0 1.0
CA B:HIS745 4.0 35.4 1.0
CE1 B:HIS745 4.0 43.2 1.0
CD2 B:LEU735 4.4 42.0 1.0
O B:GLN696 4.6 46.2 1.0
CB B:THR748 4.7 35.9 1.0
O B:ASN744 4.8 39.1 1.0
N B:THR748 4.8 26.7 1.0
C B:HIS745 4.9 35.0 1.0
CD2 B:HIS745 4.9 44.2 1.0
CB B:ASP747 5.0 29.7 1.0

Reference:

G.N.Maertens, N.J.Cook, W.Wang, S.Hare, S.S.Gupta, I.Oztop, K.Lee, V.E.Pye, O.Cosnefroy, A.P.Snijders, V.N.Kewalramani, A.Fassati, A.Engelman, P.Cherepanov. Structural Basis For Nuclear Import of Splicing Factors By Human Transportin 3. Proc.Natl.Acad.Sci.Usa V. 111 2728 2014.
ISSN: ISSN 0027-8424
PubMed: 24449914
DOI: 10.1073/PNAS.1320755111
Page generated: Sun Dec 13 23:29:17 2020

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