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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 4nsy:

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

Calcium (Ca) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine 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 Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Wild-Type Lysobacter Enzymogenes Lysc Endoproteinase Covalently Inhibited By Tlck, PDB code: 4nsy:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 4nsy

Go back to Chlorine Binding Sites List in 4nsy
Chlorine 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 Chlorine with other atoms in the Cl 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
A:Cl302

b:12.5
occ:1.00
HE2 A:HIS210 2.3 11.2 1.0
HE2 B:HIS210 2.3 12.5 1.0
H4 B:2OY301 2.8 11.9 1.0
H4 A:2OY301 2.8 11.8 1.0
H6 B:2OY301 3.0 10.3 1.0
H6 A:2OY301 3.0 11.1 1.0
O A:HOH768 3.0 26.1 1.0
O A:HOH623 3.2 17.7 1.0
NE2 A:HIS210 3.2 9.3 1.0
NE2 B:HIS210 3.2 10.4 1.0
C4 B:2OY301 3.5 9.9 1.0
C4 A:2OY301 3.5 9.8 1.0
C6 B:2OY301 3.6 8.6 1.0
C6 A:2OY301 3.6 9.2 1.0
HB3 B:HIS57 3.9 8.7 1.0
HB3 A:HIS57 3.9 9.1 1.0
HD2 A:HIS210 4.0 10.8 1.0
CD2 A:HIS210 4.0 9.0 1.0
CD2 B:HIS210 4.0 6.9 1.0
HD2 B:HIS210 4.0 8.2 1.0
HB2 A:HIS57 4.1 9.1 1.0
HB2 B:HIS57 4.1 8.7 1.0
CE1 A:HIS210 4.2 8.7 1.0
CE1 B:HIS210 4.2 8.2 1.0
HE1 B:HIS210 4.3 9.8 1.0
HE1 A:HIS210 4.3 10.4 1.0
CB B:HIS57 4.4 7.3 1.0
CB A:HIS57 4.4 7.6 1.0
HD1 B:HIS57 4.8 8.4 1.0
CG B:HIS57 4.8 7.8 1.0
C2 B:2OY301 4.8 10.2 1.0
CG A:HIS57 4.8 7.2 1.0
C2 A:2OY301 4.8 10.9 1.0
H13 B:2OY301 4.8 16.0 1.0
HD1 A:HIS57 4.9 9.2 1.0
O A:HOH486 4.9 17.6 1.0
C7 B:2OY301 5.0 9.6 1.0
C7 A:2OY301 5.0 8.4 1.0
ND1 B:HIS57 5.0 7.0 1.0
O B:HOH471 5.0 18.0 1.0
ND1 A:HIS57 5.0 7.7 1.0

Chlorine binding site 2 out of 2 in 4nsy

Go back to Chlorine Binding Sites List in 4nsy
Chlorine 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 Chlorine with other atoms in the Cl 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
A:Cl303

b:14.3
occ:1.00
O A:HOH760 2.2 28.7 1.0
O A:HOH859 2.4 28.7 1.0
O A:HOH866 2.4 36.4 1.0
O A:HOH860 2.4 33.0 1.0
OD1 A:ASN151 2.5 8.3 1.0
O A:HOH780 2.5 36.7 1.0
CG A:ASN151 3.5 8.2 1.0
HD21 A:ASN151 3.5 12.3 1.0
ND2 A:ASN151 3.9 10.3 1.0
O A:HOH699 4.2 27.2 1.0
O A:HOH708 4.2 30.8 1.0
HA A:ASN151 4.4 8.4 1.0
O B:HOH841 4.4 39.5 1.0
O A:HOH567 4.5 22.6 1.0
O A:HOH456 4.5 12.9 1.0
O A:HOH598 4.5 28.1 1.0
O A:HOH733 4.5 31.3 1.0
O A:HOH443 4.7 11.3 1.0
HD22 A:ASN151 4.8 12.3 1.0
O A:HOH881 4.8 15.7 0.5
CB A:ASN151 4.8 8.4 1.0
O A:ASN151 4.8 8.2 1.0
CA A:ASN151 5.0 7.0 1.0

Reference:

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
Page generated: Sat Dec 12 10:59:13 2020

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