Sodium in PDB 3njo: X-Ray Crystal Structure of the PYR1-Pyrabactin A Complex

The structure of X-Ray Crystal Structure of the PYR1-Pyrabactin A Complex, PDB code: 3njo was solved by E.S.Burgie, C.A.Bingman, G.N.Phillips Jr., F.C.Peterson, B.F.Volkman, S.R.Cutler, D.R.Jensen, Center For Eukaryotic Structural Genomics(Cesg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.05 / 2.47
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	60.307, 60.307, 527.599, 90.00, 90.00, 120.00
R / Rfree (%)	22.2 / 26.5

The structure of X-Ray Crystal Structure of the PYR1-Pyrabactin A Complex also contains other interesting chemical elements:

Bromine	(Br)	3 atoms
Chlorine	(Cl)	1 atom

The binding sites of Sodium atom in the X-Ray Crystal Structure of the PYR1-Pyrabactin A Complex (pdb code 3njo). 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 X-Ray Crystal Structure of the PYR1-Pyrabactin A Complex, PDB code: 3njo:

Sodium binding site 1 out of 1 in the X-Ray Crystal Structure of the PYR1-Pyrabactin A Complex


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of X-Ray Crystal Structure of the PYR1-Pyrabactin A Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Na193 b:60.3 occ:1.00 O B:HOH202 2.6 55.3 1.0 OG B:SER88 2.6 78.2 1.0 N A:GLY86 2.9 61.3 1.0 OG A:SER85 3.2 71.4 1.0 CB B:SER88 3.5 72.9 1.0 CA A:GLY86 3.5 55.3 1.0 C A:SER85 3.8 62.6 1.0 N A:LEU87 3.8 58.8 1.0 C A:GLY86 3.8 56.0 1.0 O A:LEU87 3.9 80.8 1.0 CA A:SER85 4.0 64.9 1.0 CB A:SER85 4.2 66.3 1.0 C A:LEU87 4.5 65.9 1.0 O A:GLY86 4.6 62.5 1.0 CA A:LEU87 4.8 60.3 1.0 OD1 B:ASP154 4.8 0.1 1.0 O A:SER85 4.9 61.4 1.0 CA B:SER88 4.9 64.5 1.0

F.C.Peterson, E.S.Burgie, S.Y.Park, D.R.Jensen, J.J.Weiner, C.A.Bingman, C.E.Chang, S.R.Cutler, G.N.Phillips, B.F.Volkman. Structural Basis For Selective Activation of Aba Receptors. Nat.Struct.Mol.Biol. V. 17 1109 2010.
ISSN: ISSN 1545-9993
PubMed: 20729860
DOI: 10.1038/NSMB.1898