Sodium in PDB 4rko: Crystal Structure of Thrombin Mutant S195T Bound with Ppack

All present enzymatic activity of Crystal Structure of Thrombin Mutant S195T Bound with Ppack:
3.4.21.5;

The structure of Crystal Structure of Thrombin Mutant S195T Bound with Ppack, PDB code: 4rko was solved by A.L.Pelc, Z.Chen, D.W.Gohara, A.D.Vogt, N.Pozzi, E.Di Cera, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 1.84
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.593, 73.310, 48.706, 90.00, 113.43, 90.00
R / Rfree (%)	16.6 / 20.2

The binding sites of Sodium atom in the Crystal Structure of Thrombin Mutant S195T Bound with Ppack (pdb code 4rko). 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 Thrombin Mutant S195T Bound with Ppack, PDB code: 4rko:

Sodium binding site 1 out of 1 in the Crystal Structure of Thrombin Mutant S195T Bound with Ppack


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 Thrombin Mutant S195T Bound with Ppack within 5.0Å range: probe atom residue distance (Å) B Occ B:Na305 b:32.4 occ:1.00 O B:ARG221A 2.2 28.7 1.0 O B:LYS224 2.3 31.0 1.0 O B:HOH465 2.3 31.8 1.0 O B:HOH464 2.4 30.3 1.0 O B:HOH463 2.4 40.6 1.0 O B:HOH448 2.8 33.9 1.0 C B:ARG221A 3.3 30.1 1.0 C B:LYS224 3.4 31.1 1.0 N B:LYS224 3.8 35.1 1.0 N B:ARG221A 3.8 27.9 1.0 O B:HOH407 3.9 32.2 1.0 CA B:LYS224 4.1 33.9 1.0 O B:TYR184A 4.1 30.1 1.0 C B:ASP221 4.1 30.1 1.0 O B:HOH450 4.1 35.3 1.0 N B:ASP222 4.2 30.0 1.0 CA B:ARG221A 4.2 29.7 1.0 N B:GLY223 4.3 33.4 1.0 O B:HOH428 4.3 29.2 1.0 CA B:ASP222 4.3 33.1 1.0 CA B:ASP221 4.4 29.9 1.0 CB B:LYS224 4.4 36.4 1.0 N B:TYR225 4.4 27.4 1.0 C B:ASP222 4.5 34.2 1.0 O B:ASP221 4.6 30.3 1.0 O B:HOH457 4.7 42.6 1.0 CA B:TYR225 4.7 27.7 1.0 OD1 B:ASP221 4.7 34.4 1.0 C B:GLY223 4.9 33.5 1.0 CD1 B:TYR225 4.9 29.8 1.0 O B:HOH433 5.0 35.6 1.0

L.A.Pelc, Z.Chen, D.W.Gohara, A.D.Vogt, N.Pozzi, E.Di Cera. Why Ser and Not Thr Brokers Catalysis in the Trypsin Fold. Biochemistry V. 54 1457 2015.
ISSN: ISSN 0006-2960
PubMed: 25664608
DOI: 10.1021/ACS.BIOCHEM.5B00014