Sodium in PDB 4a60: Crystal Structure of Human Testis-Specific Fatty Acid Binding Protein 9 (FABP9)

The structure of Crystal Structure of Human Testis-Specific Fatty Acid Binding Protein 9 (FABP9), PDB code: 4a60 was solved by J.R.C.Muniz, W.Kiyani, L.Shrestha, D.S.Froese, T.Krojer, M.Vollmar, C.H.Arrowsmith, A.M.Edwards, J.Weigelt, C.Bountra, F.Von Delft, W.W.Yue, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.60 / 1.53
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	75.486, 75.486, 113.298, 90.00, 90.00, 90.00
R / Rfree (%)	16.9 / 18.3

The binding sites of Sodium atom in the Crystal Structure of Human Testis-Specific Fatty Acid Binding Protein 9 (FABP9) (pdb code 4a60). 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 Crystal Structure of Human Testis-Specific Fatty Acid Binding Protein 9 (FABP9), PDB code: 4a60:

Sodium binding site 1 out of 1 in the Crystal Structure of Human Testis-Specific Fatty Acid Binding Protein 9 (FABP9)


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Human Testis-Specific Fatty Acid Binding Protein 9 (FABP9) within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1132 b:21.0 occ:1.00 OG A:SER56 3.0 21.0 1.0 O A:HOH2100 3.1 41.1 1.0 OE1 A:GLN59 3.2 28.5 1.0 CB A:SER56 3.9 21.7 1.0 CB A:PHE58 3.9 19.7 1.0 CD A:GLN59 4.0 26.4 1.0 CG A:GLN59 4.1 21.4 1.0 CB A:ALA34 4.1 20.4 1.0 O1 A:EDO1134 4.2 65.0 1.0 CD2 A:PHE58 4.2 19.9 1.0 CG2 A:VAL37 4.5 24.1 1.0 CG A:PHE58 4.6 18.6 1.0 CB A:GLN59 4.7 21.1 1.0 CA A:PHE58 4.7 19.6 1.0 C A:PHE58 4.7 22.2 1.0 CA A:ALA34 4.7 18.5 1.0 N A:GLN59 4.7 19.4 1.0 N A:PHE58 4.8 19.5 1.0 O A:ALA34 5.0 22.6 1.0

J.R.C.Muniz, W.Kiyani, L.Shrestha, D.S.Froese, T.Krojer, M.Vollmar, C.H.Arrowsmith, A.M.Edwards, J.Weigelt, C.Bountra, F.Von Delft, W.W.Yue. The Crystal Structure of the Human FABP9A To Be Published.