Chlorine in PDB 4a5t: Structural Basis For the Conformational Modulation

All present enzymatic activity of Structural Basis For the Conformational Modulation:
3.4.21.7;

The structure of Structural Basis For the Conformational Modulation, PDB code: 4a5t was solved by Y.Xue, C.Bodin, K.Olsson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.80 / 3.49
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	118.460, 118.460, 179.250, 90.00, 90.00, 90.00
R / Rfree (%)	20.85 / 25.01

The binding sites of Chlorine atom in the Structural Basis For the Conformational Modulation (pdb code 4a5t). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structural Basis For the Conformational Modulation, PDB code: 4a5t:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structural Basis For the Conformational Modulation


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structural Basis For the Conformational Modulation within 5.0Å range: probe atom residue distance (Å) B Occ S:Cl1001 b:33.9 occ:1.00 CB S:ARG68 3.2 33.6 1.0 N S:ARG68 3.2 35.9 1.0 CZ S:PHE419 3.2 49.3 1.0 NH2 S:ARG426 3.2 20.8 1.0 NZ S:LYS392 3.3 75.2 1.0 CE1 S:PHE419 3.5 50.2 1.0 CG1 S:ILE67 3.7 40.5 1.0 CA S:ARG68 3.8 35.5 1.0 NE S:ARG426 3.8 42.5 1.0 CD S:LYS392 3.9 63.5 1.0 CZ S:ARG426 4.0 49.0 1.0 C S:ILE67 4.1 40.0 1.0 CA S:ILE67 4.1 35.9 1.0 CE S:LYS392 4.2 69.3 1.0 CB S:HIS390 4.3 50.5 1.0 CG S:ARG68 4.4 35.9 1.0 CD S:ARG68 4.4 36.8 1.0 CE2 S:PHE419 4.4 51.8 1.0 CD1 S:ILE67 4.5 53.1 1.0 CB S:ILE67 4.6 38.6 1.0 CD1 S:PHE419 4.9 49.9 1.0 C S:ARG68 5.0 40.1 1.0

Chlorine binding site 2 out of 2 in the Structural Basis For the Conformational Modulation


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structural Basis For the Conformational Modulation within 5.0Å range: probe atom residue distance (Å) B Occ S:Cl1002 b:37.9 occ:1.00 NH2 S:ARG153 2.8 62.6 1.0 NE S:ARG153 3.5 57.5 1.0 CZ S:ARG153 3.5 72.4 1.0 NH2 S:ARG117 3.6 90.2 1.0 NE S:ARG117 3.7 91.7 1.0 OH S:TYR146 3.8 61.9 1.0 CZ S:ARG117 4.0 0.3 1.0 CB S:ARG117 4.0 55.9 1.0 CE1 S:TYR146 4.3 58.3 1.0 CZ S:TYR146 4.5 63.2 1.0 CG S:ARG117 4.6 70.8 1.0 CD S:ARG117 4.7 84.6 1.0 CD S:ARG153 4.8 55.8 1.0 NH1 S:ARG153 4.8 61.8 1.0

Y.Xue, C.Bodin, K.Olsson. Crystal Structure of the Native Plasminogen Reveals An Activation-Resistant Compact Conformation. J. Thromb. Haemost. V. 10 1385 2012.
ISSN: ISSN 1538-7933
PubMed: 22540246
DOI: 10.1111/J.1538-7836.2012.04765.X