Sodium in PDB 7a0a: Crystal Structure of Mouse Csad in Apo Form

All present enzymatic activity of Crystal Structure of Mouse Csad in Apo Form:
4.1.1.11; 4.1.1.29;

The structure of Crystal Structure of Mouse Csad in Apo Form, PDB code: 7a0a was solved by E.Mahootchi, A.Raasakka, J.Haavik, P.Kursula, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.02 / 2.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	73.06, 114.88, 113.76, 90, 95.8, 90
R / Rfree (%)	24.3 / 29.2

The binding sites of Sodium atom in the Crystal Structure of Mouse Csad in Apo Form (pdb code 7a0a). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 3 binding sites of Sodium where determined in the Crystal Structure of Mouse Csad in Apo Form, PDB code: 7a0a:
Jump to Sodium binding site number: 1; 2; 3;

Sodium binding site 1 out of 3 in the Crystal Structure of Mouse Csad in Apo Form


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 Mouse Csad in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Na502 b:27.9 occ:1.00 O A:PHE401 2.4 57.8 1.0 O A:ILE395 2.8 49.8 1.0 O A:ARG398 3.0 47.2 1.0 HA A:LYS396 3.1 57.9 1.0 O A:LYS396 3.6 52.5 1.0 C A:PHE401 3.6 47.3 1.0 CA A:LYS396 3.8 48.3 1.0 HA A:GLU402 3.9 55.3 1.0 C A:LYS396 3.9 47.4 1.0 C A:ILE395 3.9 50.9 1.0 H A:PHE401 4.0 66.2 1.0 HB2 A:PHE401 4.1 61.8 1.0 C A:ARG398 4.2 55.5 1.0 HA A:GLU399 4.3 73.4 1.0 HG23 A:ILE395 4.3 59.5 1.0 N A:LYS396 4.3 47.5 1.0 HG22 A:ILE395 4.5 59.5 1.0 N A:PHE401 4.5 55.2 1.0 H A:ARG398 4.5 61.8 1.0 CA A:PHE401 4.5 54.0 1.0 N A:GLU402 4.6 48.8 1.0 CA A:GLU402 4.6 46.1 1.0 N A:ARG398 4.7 51.5 1.0 CB A:PHE401 4.8 51.5 1.0 N A:LYS397 4.8 41.6 1.0 H A:GLY400 4.8 83.2 1.0 CG2 A:ILE395 4.9 49.6 1.0

Sodium binding site 2 out of 3 in the Crystal Structure of Mouse Csad in Apo Form


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of Mouse Csad in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ C:Na501 b:51.0 occ:1.00 O C:PHE401 2.8 64.4 1.0 O C:ARG398 2.8 55.1 1.0 O C:ILE395 3.0 54.8 1.0 HA C:LYS396 3.3 64.3 1.0 O C:LYS396 3.6 56.3 1.0 HA C:GLU399 3.9 80.3 1.0 C C:LYS396 4.0 51.1 1.0 C C:ARG398 4.0 63.9 1.0 CA C:LYS396 4.0 53.6 1.0 C C:PHE401 4.0 51.2 1.0 C C:ILE395 4.1 50.7 1.0 H C:PHE401 4.2 73.7 1.0 HA C:GLU402 4.2 58.0 1.0 HB2 C:PHE401 4.5 64.2 1.0 N C:LYS396 4.5 55.5 1.0 H C:ARG398 4.5 71.9 1.0 HG23 C:ILE395 4.6 65.6 1.0 H C:GLY400 4.6 77.0 1.0 CA C:GLU399 4.7 66.9 1.0 N C:ARG398 4.7 59.9 1.0 N C:PHE401 4.7 61.4 1.0 HG22 C:ILE395 4.7 65.6 1.0 N C:GLU399 4.7 72.0 1.0 CA C:PHE401 4.9 54.5 1.0 N C:LYS397 4.9 42.7 1.0 N C:GLU402 4.9 51.8 1.0 CA C:ARG398 5.0 59.1 1.0 CA C:GLU402 5.0 48.3 1.0

Sodium binding site 3 out of 3 in the Crystal Structure of Mouse Csad in Apo Form


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 3 of Crystal Structure of Mouse Csad in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ D:Na501 b:55.9 occ:1.00 O D:PHE401 2.5 71.8 1.0 O D:ARG398 2.7 61.6 1.0 O D:ILE395 3.3 51.3 1.0 HA D:LYS396 3.5 67.4 1.0 HA D:GLU399 3.6 89.8 1.0 O D:LYS396 3.6 47.8 1.0 C D:PHE401 3.7 66.9 1.0 H D:PHE401 3.7 80.0 1.0 C D:ARG398 3.8 63.5 1.0 C D:LYS396 4.1 53.7 1.0 HB2 D:PHE401 4.1 71.3 1.0 HA D:GLU402 4.1 81.9 1.0 CA D:LYS396 4.2 56.2 1.0 N D:PHE401 4.3 66.6 1.0 H D:GLY400 4.3 87.3 1.0 CA D:GLU399 4.4 74.8 1.0 C D:ILE395 4.4 50.1 1.0 CA D:PHE401 4.5 63.5 1.0 H D:ARG398 4.5 67.3 1.0 N D:GLU399 4.5 70.8 1.0 N D:ARG398 4.6 56.1 1.0 N D:GLU402 4.7 68.1 1.0 N D:GLY400 4.7 72.8 1.0 CB D:PHE401 4.8 59.4 1.0 HG23 D:ILE395 4.8 65.5 1.0 N D:LYS396 4.8 55.1 1.0 CA D:ARG398 4.8 56.7 1.0 CA D:GLU402 4.9 68.2 1.0 C D:GLU399 4.9 68.6 1.0 N D:LYS397 5.0 56.7 1.0

E.Mahootchi, A.Raasakka, W.Luan, G.Muruganandam, R.Loris, J.Haavik, P.Kursula. The Structure of Cysteine Sulphinic Acid Decarboxylase Reveals Structural Determinants For Substrate Specificity of Pyridoxal Phosphate-Dependent Decarboxylases To Be Published.