Sodium in PDB 4ka9: Crystal Structure Analysis of Single Amino Acid Deletion Mutations in Egfp

The structure of Crystal Structure Analysis of Single Amino Acid Deletion Mutations in Egfp, PDB code: 4ka9 was solved by J.A.J.Arpino, P.Rizkallah, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.88 / 1.58
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	91.870, 66.660, 45.290, 90.00, 108.76, 90.00
R / Rfree (%)	17.3 / 21

The structure of Crystal Structure Analysis of Single Amino Acid Deletion Mutations in Egfp also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Sodium atom in the Crystal Structure Analysis of Single Amino Acid Deletion Mutations in Egfp (pdb code 4ka9). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure Analysis of Single Amino Acid Deletion Mutations in Egfp, PDB code: 4ka9:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Crystal Structure Analysis of Single Amino Acid Deletion Mutations in Egfp


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure Analysis of Single Amino Acid Deletion Mutations in Egfp within 5.0Å range: probe atom residue distance (Å) B Occ A:Na311 b:16.5 occ:1.00 O A:HOH577 1.5 56.9 1.0 O A:HOH530 2.1 32.0 1.0 O A:HOH588 2.1 37.8 1.0 NE2 A:HIS25 2.3 26.2 1.0 CE1 A:HIS25 2.7 30.6 1.0 OE2 A:GLU132 2.7 33.7 1.0 OE1 A:GLU132 3.0 44.5 1.0 CD A:GLU132 3.3 36.1 1.0 CD2 A:HIS25 3.7 25.4 1.0 O A:HOH648 3.9 47.5 1.0 ND1 A:HIS25 4.0 28.4 1.0 O A:HOH545 4.4 34.4 1.0 CG A:HIS25 4.5 25.5 1.0 O A:HOH512 4.7 28.6 1.0 CG A:GLU132 4.8 32.4 1.0 CD1 A:LEU137 5.0 18.0 1.0

Sodium binding site 2 out of 2 in the Crystal Structure Analysis of Single Amino Acid Deletion Mutations in Egfp


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure Analysis of Single Amino Acid Deletion Mutations in Egfp within 5.0Å range: probe atom residue distance (Å) B Occ A:Na314 b:13.0 occ:1.00 O A:HOH654 2.0 32.6 1.0 O A:HOH652 2.0 37.0 1.0 O A:HOH653 2.0 33.6 1.0 CE A:LYS3 4.0 23.0 0.5 CD A:LYS3 4.1 22.9 0.5 O A:SER2 4.2 27.1 1.0 N A:VAL1 4.2 27.0 1.0 CE A:LYS3 4.3 23.5 0.5 O A:HOH562 4.3 36.5 1.0 CD A:LYS3 4.7 21.5 0.5 CA A:VAL1 4.8 24.7 1.0 NZ A:LYS3 4.9 21.4 0.5

J.A.J.Arpino, L.M.Halliwell, N.H.Zulkifli, P.J.Rizkallah, D.D.Jones. Single Amino Acid Deletion Mutagenesis; Engineering Gfp Through Polypeptide Backbone Mutations. To Be Published.
DOI: 10.1016/J.STR.2014.03.014