Calcium in PDB 4nsy: Wild-Type Lysobacter Enzymogenes Lysc Endoproteinase Covalently Inhibited By Tlck

All present enzymatic activity of Wild-Type Lysobacter Enzymogenes Lysc Endoproteinase Covalently Inhibited By Tlck:
3.4.21.50;

The structure of Wild-Type Lysobacter Enzymogenes Lysc Endoproteinase Covalently Inhibited By Tlck, PDB code: 4nsy 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)	33.99 / 1.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.579, 135.810, 45.587, 90.00, 97.19, 90.00
R / Rfree (%)	16.4 / 20.8

The structure of Wild-Type Lysobacter Enzymogenes Lysc Endoproteinase Covalently Inhibited By Tlck also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Calcium atom in the Wild-Type Lysobacter Enzymogenes Lysc Endoproteinase Covalently Inhibited By Tlck (pdb code 4nsy). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Wild-Type Lysobacter Enzymogenes Lysc Endoproteinase Covalently Inhibited By Tlck, PDB code: 4nsy:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Wild-Type Lysobacter Enzymogenes Lysc Endoproteinase Covalently Inhibited By Tlck


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Wild-Type Lysobacter Enzymogenes Lysc Endoproteinase Covalently Inhibited By Tlck within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca302 b:32.2 occ:1.00 OD2 B:ASP246 2.4 16.2 1.0 O B:HOH706 2.4 41.8 1.0 O B:HOH703 2.5 31.1 1.0 O B:HOH782 2.6 32.4 1.0 O B:HOH847 2.6 32.3 1.0 HB3 B:ASP246 3.4 13.5 1.0 CG B:ASP246 3.5 13.3 1.0 HH21 B:ARG243 3.6 17.7 1.0 HB3 B:SER240 3.8 18.1 1.0 O B:HOH648 3.9 38.8 1.0 CB B:ASP246 4.0 11.3 1.0 NH2 B:ARG243 4.3 14.7 1.0 HH22 B:ARG243 4.4 17.7 1.0 HA B:ASP246 4.4 15.2 1.0 O B:HOH491 4.6 15.5 1.0 OD1 B:ASP246 4.6 12.7 1.0 CB B:SER240 4.7 15.1 1.0 HB2 B:ASP246 4.7 13.5 1.0 HB2 B:SER240 4.7 18.1 1.0 O B:HOH645 4.7 23.9 1.0 CA B:ASP246 4.8 12.7 1.0 O B:HOH657 4.9 29.4 1.0 O B:HOH781 4.9 26.9 1.0

Calcium binding site 2 out of 2 in the Wild-Type Lysobacter Enzymogenes Lysc Endoproteinase Covalently Inhibited By Tlck


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Wild-Type Lysobacter Enzymogenes Lysc Endoproteinase Covalently Inhibited By Tlck within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca303 b:16.4 occ:1.00 O B:HOH660 2.3 22.4 1.0 OD1 B:ASN151 2.4 9.1 1.0 O B:HOH749 2.4 25.8 1.0 O B:HOH830 2.4 43.5 1.0 O B:HOH753 2.5 24.2 1.0 O B:HOH824 3.1 40.8 1.0 CG B:ASN151 3.4 8.4 1.0 HD21 B:ASN151 3.5 12.1 1.0 ND2 B:ASN151 3.9 10.1 1.0 O B:HOH865 3.9 33.4 1.0 O B:HOH690 4.2 24.6 1.0 HA B:ASN151 4.3 7.7 1.0 O A:HOH621 4.4 26.6 1.0 O B:HOH559 4.4 26.2 1.0 O A:HOH829 4.5 31.8 1.0 O A:HOH702 4.5 37.5 1.0 O B:HOH479 4.5 13.7 1.0 O B:HOH741 4.7 12.9 1.0 HD22 B:ASN151 4.7 12.1 1.0 CB B:ASN151 4.8 7.6 1.0 O B:ASN151 4.8 8.2 1.0 O B:HOH723 4.9 26.8 1.0 O A:HOH694 4.9 33.0 1.0 CA B:ASN151 5.0 6.4 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