Cobalt in PDB 6zek: Crystal Structure of Mouse Csad

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

The structure of Crystal Structure of Mouse Csad, PDB code: 6zek 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)	46.89 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	72.94, 113.26, 113.37, 90, 95.81, 90
R / Rfree (%)	17.9 / 23.5

The structure of Crystal Structure of Mouse Csad also contains other interesting chemical elements:

Chlorine

(Cl)

13 atoms

The binding sites of Cobalt atom in the Crystal Structure of Mouse Csad (pdb code 6zek). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 4 binding sites of Cobalt where determined in the Crystal Structure of Mouse Csad, PDB code: 6zek:
Jump to Cobalt binding site number: 1; 2; 3; 4;

Cobalt binding site 1 out of 4 in the Crystal Structure of Mouse Csad


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of Mouse Csad within 5.0Å range: probe atom residue distance (Å) B Occ A:Co502 b:48.6 occ:1.00 O A:ARG398 2.4 30.5 1.0 O A:PHE401 2.6 32.5 1.0 O A:ILE395 2.7 30.9 1.0 O A:HOH767 3.0 43.9 1.0 HA A:LYS396 3.1 42.1 1.0 O A:LYS396 3.2 37.6 1.0 H A:PHE401 3.5 37.7 1.0 C A:ARG398 3.5 36.4 1.0 C A:LYS396 3.6 31.9 1.0 H A:ARG398 3.6 43.8 1.0 HB2 A:PHE401 3.7 37.8 1.0 C A:PHE401 3.7 33.2 1.0 CA A:LYS396 3.8 35.1 1.0 C A:ILE395 3.8 34.9 1.0 N A:ARG398 4.0 36.5 1.0 HA A:GLU399 4.0 42.7 1.0 N A:PHE401 4.2 31.4 1.0 N A:LYS396 4.3 31.2 1.0 CA A:PHE401 4.3 29.7 1.0 CA A:ARG398 4.4 33.7 1.0 HA A:GLU402 4.4 36.0 1.0 CB A:PHE401 4.4 31.5 1.0 N A:GLU399 4.5 34.8 1.0 HG23 A:ILE395 4.5 34.6 1.0 N A:LYS397 4.5 33.2 1.0 H A:GLY400 4.6 47.9 1.0 CA A:GLU399 4.6 35.6 1.0 C A:LYS397 4.7 38.4 1.0 HB2 A:ARG398 4.7 41.4 1.0 HG22 A:ILE395 4.8 34.6 1.0 N A:GLU402 4.8 26.1 1.0 N A:GLY400 4.8 39.9 1.0 HB3 A:PHE401 4.9 37.8 1.0 O A:HOH741 4.9 28.3 1.0 C A:GLU399 4.9 42.1 1.0 HD2 A:PHE401 5.0 40.6 1.0

Cobalt binding site 2 out of 4 in the Crystal Structure of Mouse Csad


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Crystal Structure of Mouse Csad within 5.0Å range: probe atom residue distance (Å) B Occ B:Co502 b:39.6 occ:0.64 O B:ARG398 2.4 30.1 1.0 O B:ILE395 2.6 28.1 1.0 O B:PHE401 2.7 45.0 1.0 O B:LYS396 2.8 43.1 1.0 HA B:LYS396 3.0 43.3 1.0 O B:HOH699 3.0 42.5 1.0 C B:LYS396 3.3 31.2 1.0 C B:ARG398 3.6 39.4 1.0 CA B:LYS396 3.6 36.1 1.0 C B:ILE395 3.7 32.6 1.0 H B:ARG398 3.8 35.2 1.0 HB2 B:PHE401 3.9 45.2 1.0 H B:PHE401 3.9 50.7 1.0 C B:PHE401 3.9 40.2 1.0 N B:ARG398 4.0 29.3 1.0 HA B:GLU399 4.0 53.5 1.0 N B:LYS396 4.1 34.3 1.0 O B:HOH692 4.3 31.4 1.0 N B:LYS397 4.3 30.0 1.0 HA B:GLU402 4.3 47.9 1.0 CA B:ARG398 4.4 34.3 1.0 HG23 B:ILE395 4.5 40.6 1.0 C B:LYS397 4.5 32.9 1.0 N B:GLU399 4.5 37.6 1.0 N B:PHE401 4.5 42.2 1.0 CA B:PHE401 4.6 43.0 1.0 CB B:PHE401 4.6 37.6 1.0 CA B:GLU399 4.7 44.6 1.0 HG22 B:ILE395 4.7 40.6 1.0 HB2 B:ARG398 4.8 46.8 1.0 H B:LYS397 4.9 36.0 1.0 CA B:LYS397 4.9 32.1 1.0 N B:GLU402 4.9 39.5 1.0 HB3 B:PHE401 4.9 45.2 1.0 CB B:LYS396 4.9 29.4 1.0 HA B:ILE395 5.0 35.4 1.0 HA B:LYS397 5.0 38.5 1.0 CA B:ILE395 5.0 29.5 1.0

Cobalt binding site 3 out of 4 in the Crystal Structure of Mouse Csad


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 3 of Crystal Structure of Mouse Csad within 5.0Å range: probe atom residue distance (Å) B Occ C:Co503 b:30.8 occ:0.60 O C:ARG398 2.4 31.7 1.0 O C:HOH766 2.6 39.4 1.0 O C:ILE395 2.7 33.6 1.0 O C:PHE401 2.7 27.4 1.0 HA C:LYS396 3.2 40.5 1.0 O C:LYS396 3.4 35.9 1.0 C C:ARG398 3.5 29.2 1.0 H C:PHE401 3.7 28.8 1.0 C C:LYS396 3.7 33.1 1.0 H C:ARG398 3.7 40.7 1.0 HB2 C:PHE401 3.8 34.7 1.0 C C:ILE395 3.8 31.7 1.0 C C:PHE401 3.8 29.7 1.0 CA C:LYS396 3.8 33.8 1.0 HA C:GLU399 4.0 46.1 1.0 N C:ARG398 4.0 33.9 1.0 N C:PHE401 4.3 24.0 1.0 N C:LYS396 4.3 29.1 1.0 CA C:ARG398 4.4 34.7 1.0 N C:LYS397 4.4 30.0 1.0 CA C:PHE401 4.4 27.4 1.0 N C:GLU399 4.4 35.9 1.0 HG23 C:ILE395 4.5 32.8 1.0 CB C:PHE401 4.5 28.9 1.0 HA C:GLU402 4.5 41.1 1.0 CA C:GLU399 4.6 38.4 1.0 C C:LYS397 4.6 33.2 1.0 HB2 C:ARG398 4.7 40.6 1.0 H C:GLY400 4.7 41.4 1.0 O C:HOH748 4.8 31.3 1.0 H C:LYS397 4.8 36.0 1.0 HG22 C:ILE395 4.9 32.8 1.0 HB3 C:PHE401 4.9 34.7 1.0 N C:GLU402 4.9 28.9 1.0 C C:GLU399 4.9 40.0 1.0 N C:GLY400 4.9 34.5 1.0 CA C:LYS397 5.0 34.5 1.0 HA C:ILE395 5.0 31.4 1.0

Cobalt binding site 4 out of 4 in the Crystal Structure of Mouse Csad


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 4 of Crystal Structure of Mouse Csad within 5.0Å range: probe atom residue distance (Å) B Occ D:Co502 b:41.6 occ:0.73 O D:ARG398 2.4 35.0 1.0 O D:PHE401 2.6 39.4 1.0 O D:ILE395 2.7 30.9 1.0 O D:HOH723 2.9 33.9 1.0 O D:HOH630 3.1 43.2 1.0 HA D:LYS396 3.2 48.3 1.0 O D:LYS396 3.3 39.5 1.0 C D:ARG398 3.5 37.9 1.0 C D:LYS396 3.6 37.5 1.0 H D:PHE401 3.7 46.1 1.0 HB2 D:PHE401 3.7 44.5 1.0 C D:PHE401 3.7 41.5 1.0 HA D:GLU399 3.8 53.6 1.0 CA D:LYS396 3.8 40.2 1.0 C D:ILE395 3.8 33.1 1.0 H D:ARG398 3.9 42.4 1.0 N D:ARG398 4.1 35.4 1.0 O D:HOH718 4.2 31.0 1.0 N D:PHE401 4.3 38.4 1.0 N D:LYS396 4.3 28.5 1.0 N D:LYS397 4.3 33.7 1.0 CA D:ARG398 4.4 33.9 1.0 N D:GLU399 4.4 38.5 1.0 CA D:PHE401 4.4 37.1 1.0 HA D:GLU402 4.4 38.0 1.0 CA D:GLU399 4.5 44.7 1.0 CB D:PHE401 4.5 37.1 1.0 HG23 D:ILE395 4.5 32.1 1.0 C D:LYS397 4.6 42.2 1.0 HB2 D:ARG398 4.7 48.1 1.0 H D:GLY400 4.8 55.5 1.0 N D:GLU402 4.8 33.2 1.0 H D:LYS397 4.8 40.4 1.0 HG22 D:ILE395 4.8 32.1 1.0 HB3 D:PHE401 4.8 44.5 1.0 CA D:LYS397 4.9 38.0 1.0 C D:GLU399 5.0 40.0 1.0 N D:GLY400 5.0 46.3 1.0

E.Mahootchi, A.Raasakka, W.Luan, G.Muruganandam, R.Loris, J.Haavik, P.Kursula. Structure and Substrate Specificity Determinants of the Taurine Biosynthetic Enzyme Cysteine Sulphinic Acid Decarboxylase. J.Struct.Biol. V. 213 07674 2021.
ISSN: ESSN 1095-8657
PubMed: 33253877
DOI: 10.1016/J.JSB.2020.107674