Calcium in PDB 1lne: A Structural Analysis of Metal Substitutions in Thermolysin

All present enzymatic activity of A Structural Analysis of Metal Substitutions in Thermolysin:
3.4.24.27;

The structure of A Structural Analysis of Metal Substitutions in Thermolysin, PDB code: 1lne was solved by D.R.Holland, A.C.Hausrath, D.Juers, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.70
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	93.888, 93.888, 131.164, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The structure of A Structural Analysis of Metal Substitutions in Thermolysin also contains other interesting chemical elements:

Cadmium

(Cd)

4 atoms

The binding sites of Calcium atom in the A Structural Analysis of Metal Substitutions in Thermolysin (pdb code 1lne). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the A Structural Analysis of Metal Substitutions in Thermolysin, PDB code: 1lne:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the A Structural Analysis of Metal Substitutions in Thermolysin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of A Structural Analysis of Metal Substitutions in Thermolysin within 5.0Å range: probe atom residue distance (Å) B Occ E:Ca901 b:22.3 occ:1.00 O E:GLU187 2.3 10.2 1.0 OD2 E:ASP138 2.4 14.3 1.0 O E:HOH924 2.5 10.0 1.0 OE2 E:GLU190 2.5 8.7 1.0 OE1 E:GLU190 2.5 9.0 1.0 OE1 E:GLU177 2.5 11.8 1.0 OD1 E:ASP185 2.5 10.3 1.0 CD E:GLU190 2.8 3.0 1.0 OE2 E:GLU177 2.9 12.8 1.0 CD E:GLU177 3.0 18.8 1.0 CG E:ASP138 3.3 14.5 1.0 C E:GLU187 3.4 11.8 1.0 CG E:ASP185 3.5 16.8 1.0 CD E:CD902 3.8 19.3 1.0 OD2 E:ASP185 3.8 15.1 1.0 CB E:ASP138 4.0 8.2 1.0 O E:ASP185 4.2 15.7 1.0 N E:GLU187 4.2 14.8 1.0 N E:ILE188 4.2 7.7 1.0 OD1 E:ASP138 4.2 12.9 1.0 CG E:GLU190 4.2 4.2 1.0 CA E:GLU187 4.2 11.0 1.0 CA E:ILE188 4.2 10.9 1.0 O E:HOH979 4.3 39.2 1.0 N E:GLY189 4.3 19.6 1.0 O E:HOH928 4.4 19.1 1.0 CB E:GLU187 4.5 16.7 1.0 CG E:GLU177 4.5 9.0 1.0 C E:ASP185 4.6 10.7 1.0 N E:ASP185 4.7 12.7 1.0 C E:ILE188 4.7 16.8 1.0 CB E:ASP185 4.7 13.4 1.0 O E:HOH931 4.8 11.8 1.0 CA E:ASP185 4.9 3.1 1.0 N E:GLU190 5.0 10.6 1.0 CB E:GLU177 5.0 11.0 1.0

Calcium binding site 2 out of 2 in the A Structural Analysis of Metal Substitutions in Thermolysin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of A Structural Analysis of Metal Substitutions in Thermolysin within 5.0Å range: probe atom residue distance (Å) B Occ E:Ca904 b:16.1 occ:1.00 O E:HOH909 2.2 27.6 1.0 O E:ILE197 2.2 25.8 1.0 OD1 E:ASP200 2.3 18.8 1.0 OG1 E:THR194 2.3 17.2 1.0 O E:TYR193 2.4 12.5 1.0 O E:THR194 2.4 21.4 1.0 O E:HOH932 2.5 11.5 1.0 C E:THR194 3.1 29.8 1.0 CG E:ASP200 3.3 13.1 1.0 C E:TYR193 3.4 11.6 1.0 CB E:THR194 3.4 17.5 1.0 C E:ILE197 3.4 47.3 1.0 CA E:THR194 3.6 17.8 1.0 OD2 E:ASP200 3.8 20.6 1.0 N E:THR194 3.9 13.0 1.0 CB E:ILE197 4.1 31.3 1.0 N E:PRO195 4.1 17.1 1.0 CA E:ILE197 4.2 21.7 1.0 N E:ILE197 4.3 38.4 1.0 O E:ASP200 4.4 16.0 1.0 N E:SER198 4.5 33.9 1.0 N E:ASP200 4.5 21.9 1.0 CD2 E:TYR193 4.6 14.7 1.0 CA E:TYR193 4.6 10.9 1.0 O E:GLU190 4.6 12.7 1.0 CG2 E:THR194 4.6 14.0 1.0 O E:HOH982 4.6 50.9 1.0 CA E:SER198 4.7 35.7 1.0 CB E:ASP200 4.7 12.9 1.0 CB E:TYR193 4.7 18.1 1.0 CA E:PRO195 4.7 35.4 1.0 C E:ASP200 4.7 11.7 1.0 CA E:ASP200 4.9 9.7 1.0 CG2 E:ILE197 4.9 28.6 1.0 CG E:TYR193 4.9 17.4 1.0 C E:PRO195 4.9 37.7 1.0 C E:SER198 5.0 34.6 1.0

D.R.Holland, A.C.Hausrath, D.Juers, B.W.Matthews. Structural Analysis of Zinc Substitutions in the Active Site of Thermolysin. Protein Sci. V. 4 1955 1995.
ISSN: ISSN 0961-8368
PubMed: 8535232