Chlorine in PDB 4nsv: Lysobacter Enzymogenes Lysc Endoproteinase K30R Mutant Covalently Inhibited By Tlck

All present enzymatic activity of Lysobacter Enzymogenes Lysc Endoproteinase K30R Mutant Covalently Inhibited By Tlck:
3.4.21.50;

The structure of Lysobacter Enzymogenes Lysc Endoproteinase K30R Mutant Covalently Inhibited By Tlck, PDB code: 4nsv was solved by P.Asztalos, A.Muller, W.Holke, H.Sobek, M.G.Rudolph, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.22 / 0.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.605, 135.582, 45.553, 90.00, 98.01, 90.00
R / Rfree (%)	13.8 / 15.8

The binding sites of Chlorine atom in the Lysobacter Enzymogenes Lysc Endoproteinase K30R Mutant Covalently Inhibited By Tlck (pdb code 4nsv). 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 Lysobacter Enzymogenes Lysc Endoproteinase K30R Mutant Covalently Inhibited By Tlck, PDB code: 4nsv:

Chlorine binding site 1 out of 1 in the Lysobacter Enzymogenes Lysc Endoproteinase K30R Mutant Covalently Inhibited By Tlck


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Lysobacter Enzymogenes Lysc Endoproteinase K30R Mutant Covalently Inhibited By Tlck within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl303 b:14.4 occ:1.00 HE2 B:HIS210 2.3 10.5 1.0 HE2 A:HIS210 2.3 10.3 1.0 H4 B:2OY301 2.7 9.1 1.0 H4 A:2OY301 2.7 8.5 1.0 O B:HOH722 2.8 25.5 1.0 H6 B:2OY301 3.1 7.8 1.0 H6 A:2OY301 3.1 7.9 1.0 O A:HOH824 3.1 20.6 1.0 NE2 B:HIS210 3.1 8.7 1.0 NE2 A:HIS210 3.1 8.6 1.0 C4 B:2OY301 3.4 7.6 1.0 C4 A:2OY301 3.5 7.1 1.0 C6 B:2OY301 3.6 6.5 1.0 C6 A:2OY301 3.6 6.6 1.0 HB3 B:HIS57 3.9 7.8 1.0 HB3 A:HIS57 3.9 6.8 1.0 CD2 B:HIS210 4.0 7.7 1.0 HD2 B:HIS210 4.0 9.2 1.0 CD2 A:HIS210 4.0 7.6 1.0 HD2 A:HIS210 4.0 9.2 1.0 HB2 B:HIS57 4.1 7.8 1.0 CE1 B:HIS210 4.1 8.4 1.0 HB2 A:HIS57 4.1 6.8 1.0 CE1 A:HIS210 4.1 7.9 1.0 HE1 B:HIS210 4.2 10.1 1.0 HE1 A:HIS210 4.2 9.5 1.0 CB B:HIS57 4.4 6.5 1.0 CB A:HIS57 4.4 5.7 1.0 C2 B:2OY301 4.8 7.8 1.0 C2 A:2OY301 4.8 7.4 1.0 CG B:HIS57 4.9 5.4 1.0 CG A:HIS57 4.9 5.0 1.0 HD1 A:HIS57 4.9 6.1 1.0 HD1 B:HIS57 4.9 6.6 1.0 O B:HOH475 5.0 12.6 1.0 O A:HOH499 5.0 13.1 1.0

P.Asztalos, A.Muller, W.Holke, H.Sobek, M.G.Rudolph. Atomic Resolution Structure of A Lysine-Specific Endoproteinase From Lysobacter Enzymogenes Suggests A Hydroxyl Group Bound to the Oxyanion Hole. Acta Crystallogr.,Sect.D V. 70 1832 2014.
ISSN: ISSN 0907-4449
PubMed: 25004961
DOI: 10.1107/S1399004714008463