Sodium in PDB 4mlf: Crystal Structure For the Complex of Thrombin Mutant D102N and Hirudin

All present enzymatic activity of Crystal Structure For the Complex of Thrombin Mutant D102N and Hirudin:
3.4.21.5;

The structure of Crystal Structure For the Complex of Thrombin Mutant D102N and Hirudin, PDB code: 4mlf was solved by A.D.Vogt, N.Pozzi, Z.Chen, E.Di Cera, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 2.20
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	89.506, 89.506, 133.148, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / 23.4

The binding sites of Sodium atom in the Crystal Structure For the Complex of Thrombin Mutant D102N and Hirudin (pdb code 4mlf). 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 For the Complex of Thrombin Mutant D102N and Hirudin, PDB code: 4mlf:

Sodium binding site 1 out of 1 in the Crystal Structure For the Complex of Thrombin Mutant D102N and Hirudin


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure For the Complex of Thrombin Mutant D102N and Hirudin within 5.0Å range: probe atom residue distance (Å) B Occ B:Na401 b:53.1 occ:1.00 O B:ARG221A 2.5 44.3 1.0 O B:HOH574 2.5 45.9 1.0 O B:HOH506 2.5 41.0 1.0 O B:LYS224 2.6 44.1 1.0 O B:HOH573 2.6 51.0 1.0 O B:HOH547 2.8 44.0 1.0 C B:ARG221A 3.5 45.4 1.0 C B:LYS224 3.6 44.5 1.0 N B:ARG221A 3.9 42.5 1.0 C B:ASP221 3.9 42.2 1.0 O B:HOH550 4.0 45.8 1.0 N B:LYS224 4.0 48.0 1.0 O B:HOH512 4.1 36.2 1.0 O B:TYR184A 4.1 44.5 1.0 CA B:ASP221 4.2 41.0 1.0 N B:GLY223 4.3 49.7 1.0 CA B:LYS224 4.3 46.5 1.0 N B:ASP222 4.3 47.8 1.0 CA B:ARG221A 4.4 44.3 1.0 O B:ASP221 4.4 43.2 1.0 CA B:ASP222 4.4 49.4 1.0 C B:ASP222 4.6 49.7 1.0 CB B:LYS224 4.6 46.3 1.0 N B:TYR225 4.6 43.2 1.0 OD1 B:ASP221 4.7 43.5 1.0 O B:HOH570 4.8 48.4 1.0 CA B:TYR225 4.8 41.5 1.0 N B:ASP221 4.9 40.5 1.0 CD1 B:TYR225 5.0 43.8 1.0

A.D.Vogt, N.Pozzi, Z.Chen, E.Di Cera. Essential Role of Conformational Selection in Ligand Binding. Biophys.Chem. V.186C 13 2014.
ISSN: ISSN 0301-4622
PubMed: 24113284
DOI: 10.1016/J.BPC.2013.09.003