Sodium in PDB 5a10: The Crystal Structure of Ta-Tfp, A Thiocyanate-Forming Protein Involved in Glucosinolate Breakdown (Space Group C2)

The structure of The Crystal Structure of Ta-Tfp, A Thiocyanate-Forming Protein Involved in Glucosinolate Breakdown (Space Group C2), PDB code: 5a10 was solved by J.Krausze, F.Gumz, U.Wittstock, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.875 / 1.42
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	119.390, 48.960, 68.270, 90.00, 109.71, 90.00
R / Rfree (%)	15.74 / 17.56

The binding sites of Sodium atom in the The Crystal Structure of Ta-Tfp, A Thiocyanate-Forming Protein Involved in Glucosinolate Breakdown (Space Group C2) (pdb code 5a10). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the The Crystal Structure of Ta-Tfp, A Thiocyanate-Forming Protein Involved in Glucosinolate Breakdown (Space Group C2), PDB code: 5a10:

Sodium binding site 1 out of 1 in the The Crystal Structure of Ta-Tfp, A Thiocyanate-Forming Protein Involved in Glucosinolate Breakdown (Space Group C2)


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of The Crystal Structure of Ta-Tfp, A Thiocyanate-Forming Protein Involved in Glucosinolate Breakdown (Space Group C2) within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1350 b:52.2 occ:1.00 OD2 A:ASP33 2.4 36.4 1.0 O A:HOH2063 2.9 38.3 1.0 CG A:ASP33 3.3 33.6 1.0 O A:HOH2061 3.7 29.4 1.0 CB A:ASP33 3.8 25.5 1.0 OD1 A:ASN58 3.9 29.5 1.0 O A:HOH2100 4.1 27.2 1.0 OD1 A:ASP33 4.4 37.5 1.0 N A:ASP33 4.7 21.9 1.0 CA A:ASP33 4.9 20.9 1.0

F.Gumz, J.Krausze, D.Eisenschmidt, A.Backenkohler, L.Barleben, W.Brandt, U.Wittstock. The Crystal Structure of the Thiocyanate-Forming Protein From Thlaspi Arvense, A Kelch Protein Involved in Glucosinolate Breakdown. Plant Mol.Biol. V. 89 67 2015.
ISSN: ISSN 0167-4412
PubMed: 26260516
DOI: 10.1007/S11103-015-0351-9