Sodium in PDB 9fop: Half-Closed Codh/Acs (Class 1) in the Methylated State

All present enzymatic activity of Half-Closed Codh/Acs (Class 1) in the Methylated State:
2.3.1.169;

The structure of Half-Closed Codh/Acs (Class 1) in the Methylated State also contains other interesting chemical elements:

Iron	(Fe)	24 atoms
Nickel	(Ni)	4 atoms

The binding sites of Sodium atom in the Half-Closed Codh/Acs (Class 1) in the Methylated State (pdb code 9fop). 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 Half-Closed Codh/Acs (Class 1) in the Methylated State, PDB code: 9fop:

Sodium binding site 1 out of 1 in the Half-Closed Codh/Acs (Class 1) in the Methylated State


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Half-Closed Codh/Acs (Class 1) in the Methylated State within 5.0Å range: probe atom residue distance (Å) B Occ C:Na804 b:44.4 occ:1.00 O C:PHE420 2.3 53.3 1.0 O C:ASN415 2.5 48.0 1.0 O C:GLY417 2.5 46.0 1.0 OE2 C:GLU334 2.6 52.6 1.0 O C:PHE331 2.8 45.8 1.0 C C:ASN415 3.3 41.9 1.0 CD C:GLU334 3.4 53.9 1.0 CG C:GLU334 3.5 51.5 1.0 C C:PHE420 3.5 49.9 1.0 C C:GLY417 3.6 41.1 1.0 CA C:ASN415 3.8 46.9 1.0 C C:PHE331 3.8 39.7 1.0 N C:PHE420 4.0 50.1 1.0 CB C:PHE331 4.1 34.5 1.0 N C:GLY417 4.3 45.7 1.0 CA C:PHE420 4.3 49.1 1.0 N C:GLY419 4.4 50.6 1.0 O C:THR414 4.4 50.5 1.0 N C:TYR416 4.4 42.6 1.0 N C:GLU418 4.5 41.5 1.0 CA C:GLU418 4.5 42.8 1.0 CB C:ASN415 4.5 46.3 1.0 OE1 C:GLU334 4.5 57.6 1.0 C C:TYR416 4.5 42.7 1.0 CA C:GLY417 4.5 41.4 1.0 N C:TRP421 4.6 51.3 1.0 CA C:PHE331 4.6 36.9 1.0 CB C:PHE420 4.7 49.4 1.0 OD1 C:ASN415 4.7 46.9 1.0 N C:GLU332 4.7 39.3 1.0 CB C:GLU334 4.7 49.5 1.0 CA C:TRP421 4.7 51.1 1.0 CA C:GLU332 4.8 44.3 1.0 CA C:TYR416 4.8 43.0 1.0 C C:GLU418 4.9 49.4 1.0 O C:GLU332 4.9 48.8 1.0 C C:GLY419 4.9 52.0 1.0 N C:ASN415 5.0 44.9 1.0 O C:TYR416 5.0 45.6 1.0

J.Ruickoldt, P.Wendler, H.Dobbek. The Codh/Acs Complex Caught in Action To Be Published.