Sodium in PDB 4e11: Crystal Structure of Kynurenine Formamidase From Drosophila Melanogaster

All present enzymatic activity of Crystal Structure of Kynurenine Formamidase From Drosophila Melanogaster:
3.5.1.9;

The structure of Crystal Structure of Kynurenine Formamidase From Drosophila Melanogaster, PDB code: 4e11 was solved by Q.Han, H.Robinson, J.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.84 / 2.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	75.771, 47.085, 85.683, 90.00, 90.34, 90.00
R / Rfree (%)	22.5 / 27.3

The binding sites of Sodium atom in the Crystal Structure of Kynurenine Formamidase From Drosophila Melanogaster (pdb code 4e11). 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 Kynurenine Formamidase From Drosophila Melanogaster, PDB code: 4e11:

Sodium binding site 1 out of 1 in the Crystal Structure of Kynurenine Formamidase From Drosophila Melanogaster


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 Kynurenine Formamidase From Drosophila Melanogaster within 5.0Å range: probe atom residue distance (Å) B Occ A:Na405 b:42.1 occ:0.50 OG A:SER150 2.2 35.1 0.5 O A:HOH501 2.2 40.1 1.0 O A:HOH502 2.3 39.7 1.0 CB A:SER150 3.6 36.9 0.5 CB A:SER150 3.7 36.4 0.5 O A:GLN78 3.9 32.7 1.0 N A:SER149 4.0 37.3 1.0 N A:SER150 4.0 37.3 0.5 N A:SER150 4.1 37.5 0.5 N A:PRO80 4.3 30.6 1.0 CA A:PRO80 4.4 28.9 1.0 CA A:SER150 4.5 35.4 0.5 CA A:SER150 4.5 35.7 0.5 CB A:PRO80 4.5 29.0 1.0 C A:SER149 4.6 38.6 1.0 CD A:PRO80 4.6 30.5 1.0 C A:ALA79 4.7 29.7 1.0 CG1 A:VAL148 4.7 36.0 1.0 CA A:SER149 4.8 40.4 1.0 CA A:VAL148 4.8 38.2 1.0 OG A:SER150 4.8 32.3 0.5 C A:VAL148 4.9 39.5 1.0 O A:SER150 4.9 32.8 0.5 O A:SER150 4.9 32.9 0.5

Q.Han, H.Robinson, J.Li. Biochemical Identification and Crystal Structure of Kynurenine Formamidase From Drosophila Melanogaster. Biochem.J. V. 446 253 2012.
ISSN: ISSN 0264-6021
PubMed: 22690733
DOI: 10.1042/BJ20120416