Chlorine in PDB 5jdu: Crystal Structure For Human Thrombin Mutant D189A

All present enzymatic activity of Crystal Structure For Human Thrombin Mutant D189A:
3.4.21.5;

The structure of Crystal Structure For Human Thrombin Mutant D189A, PDB code: 5jdu was solved by 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 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.429, 81.333, 146.366, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / 20.6

The binding sites of Chlorine atom in the Crystal Structure For Human Thrombin Mutant D189A (pdb code 5jdu). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure For Human Thrombin Mutant D189A, PDB code: 5jdu:

Chlorine binding site 1 out of 1 in the Crystal Structure For Human Thrombin Mutant D189A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure For Human Thrombin Mutant D189A within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl301 b:24.0 occ:1.00 O D:HOH608 3.2 20.9 1.0 N D:GLY25 3.2 17.8 1.0 O D:HOH544 3.2 27.1 1.0 O D:HOH530 3.3 24.8 1.0 NH1 D:ARG73 3.3 9.7 0.5 NH2 D:ARG73 3.4 15.5 0.5 CZ D:ARG73 3.8 15.8 0.5 CA D:ILE24 3.8 19.3 1.0 CG D:LYS70 3.9 15.9 1.0 CA D:LYS70 4.0 16.6 1.0 C D:ILE24 4.0 18.6 1.0 O D:HOH577 4.0 22.3 1.0 CA D:GLY25 4.1 17.9 1.0 CB D:LYS70 4.2 16.6 1.0 O D:GLU23 4.3 19.5 1.0 CG2 D:ILE24 4.4 22.5 1.0 NH2 D:ARG73 4.5 19.7 0.5 CB D:ILE24 4.6 20.2 1.0 N D:HIS71 4.6 17.2 1.0 O D:GLY69 4.7 16.7 1.0 O D:HOH569 4.8 20.2 1.0 N D:LYS70 4.8 17.0 1.0 C D:LYS70 4.8 17.3 1.0 N D:ILE24 4.8 19.7 1.0 CG1 D:ILE24 4.9 22.9 1.0 CD1 D:TYR117 4.9 23.8 1.0 C D:GLU23 5.0 18.9 1.0 N D:MET26 5.0 17.1 1.0 O D:HOH655 5.0 24.6 1.0

N.Pozzi, M.Zerbetto, L.Acquasaliente, S.Tescari, D.Frezzato, A.Polimeno, D.W.Gohara, E.Di Cera, V.De Filippis. Loop Electrostatics Asymmetry Modulates the Preexisting Conformational Equilibrium in Thrombin. Biochemistry V. 55 3984 2016.
ISSN: ISSN 0006-2960
PubMed: 27347732
DOI: 10.1021/ACS.BIOCHEM.6B00385