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

Enzymatic activity of 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;

Protein crystallography data

The structure of A Structural Analysis of Metal Substitutions in Thermolysin, PDB code: 1lna 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 / 1.90
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.658, 93.658, 131.564, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Other elements in 1lna:

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

Cobalt (Co) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the A Structural Analysis of Metal Substitutions in Thermolysin (pdb code 1lna). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the A Structural Analysis of Metal Substitutions in Thermolysin, PDB code: 1lna:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in 1lna

Go back to Calcium Binding Sites List in 1lna
Calcium binding site 1 out of 3 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:9.9
occ:1.00
O E:GLU187 2.3 12.6 1.0
OD2 E:ASP138 2.3 18.7 1.0
OD1 E:ASP185 2.4 11.4 1.0
OE1 E:GLU190 2.5 12.2 1.0
OE2 E:GLU190 2.5 14.2 1.0
O E:HOH925 2.5 9.2 1.0
OE1 E:GLU177 2.6 16.7 1.0
OE2 E:GLU177 2.7 10.9 1.0
CD E:GLU190 2.8 11.5 1.0
CD E:GLU177 3.0 18.7 1.0
CG E:ASP138 3.2 18.1 1.0
CG E:ASP185 3.4 24.5 1.0
C E:GLU187 3.4 21.0 1.0
CA E:CA902 3.5 12.3 1.0
OD2 E:ASP185 3.6 19.3 1.0
O E:HOH982 3.7 72.8 1.0
CB E:ASP138 4.0 6.3 1.0
N E:GLU187 4.1 18.4 1.0
O E:ASP185 4.1 20.5 1.0
OD1 E:ASP138 4.2 12.9 1.0
CA E:GLU187 4.2 18.8 1.0
CG E:GLU190 4.3 9.1 1.0
N E:ILE188 4.3 14.3 1.0
CA E:ILE188 4.4 11.3 1.0
N E:GLY189 4.4 21.3 1.0
O E:HOH929 4.4 22.3 1.0
CG E:GLU177 4.5 9.7 1.0
CB E:GLU187 4.5 20.4 1.0
C E:ASP185 4.5 16.1 1.0
O E:HOH905 4.6 21.8 1.0
CB E:ASP185 4.6 17.9 1.0
N E:ASP185 4.7 12.8 1.0
C E:ILE188 4.8 22.9 1.0
N E:GLU190 4.8 11.1 1.0
CA E:ASP185 4.9 12.4 1.0
CB E:GLU177 5.0 9.7 1.0

Calcium binding site 2 out of 3 in 1lna

Go back to Calcium Binding Sites List in 1lna
Calcium binding site 2 out of 3 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:Ca902

b:12.3
occ:1.00
OE2 E:GLU190 2.0 14.2 1.0
O E:HOH909 2.1 16.9 1.0
O E:HOH905 2.1 21.8 1.0
OD2 E:ASP185 2.2 19.3 1.0
OE2 E:GLU177 2.3 10.9 1.0
O E:ASN183 2.5 19.5 1.0
CD E:GLU177 3.1 18.7 1.0
CG E:ASP185 3.1 24.5 1.0
CD E:GLU190 3.2 11.5 1.0
CA E:CA901 3.5 9.9 1.0
OD1 E:ASP185 3.6 11.4 1.0
OE1 E:GLU177 3.6 16.7 1.0
CG E:GLU190 3.6 9.1 1.0
C E:ASN183 3.7 45.9 1.0
N E:ASP185 4.0 12.8 1.0
O E:LYS182 4.0 32.7 1.0
O E:HOH982 4.1 72.8 1.0
OD2 E:ASP191 4.1 22.6 1.0
OE1 E:GLU190 4.1 12.2 1.0
CG E:GLU177 4.1 9.7 1.0
CA E:PRO184 4.1 17.1 1.0
C E:PRO184 4.2 25.5 1.0
OD1 E:ASP191 4.2 21.6 1.0
CB E:ASP185 4.3 17.9 1.0
N E:PRO184 4.4 21.4 1.0
CG E:ASP191 4.5 16.6 1.0
CB E:ASN183 4.6 54.3 1.0
CA E:ASN183 4.7 28.7 1.0
CA E:ASP185 4.8 12.4 1.0
O E:PRO184 4.8 20.4 1.0

Calcium binding site 3 out of 3 in 1lna

Go back to Calcium Binding Sites List in 1lna
Calcium binding site 3 out of 3 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 3 of A Structural Analysis of Metal Substitutions in Thermolysin within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Ca904

b:20.8
occ:1.00
O E:ILE197 2.3 38.1 1.0
OD1 E:ASP200 2.4 22.8 1.0
O E:THR194 2.4 16.2 1.0
OG1 E:THR194 2.4 19.8 1.0
O E:TYR193 2.5 12.7 1.0
O E:HOH988 2.5 26.5 1.0
O E:HOH932 2.6 13.7 1.0
C E:THR194 3.1 40.2 1.0
CG E:ASP200 3.4 20.7 1.0
C E:ILE197 3.4 53.0 1.0
C E:TYR193 3.4 17.9 1.0
CB E:THR194 3.5 25.7 1.0
CA E:THR194 3.6 17.4 1.0
OD2 E:ASP200 3.7 22.3 1.0
N E:THR194 3.9 16.6 1.0
CA E:ILE197 4.1 28.2 1.0
N E:PRO195 4.1 19.6 1.0
N E:ILE197 4.2 44.9 1.0
CB E:ILE197 4.2 42.8 1.0
O E:ASP200 4.4 19.8 1.0
O E:HOH984 4.4 42.2 1.0
N E:SER198 4.4 30.0 1.0
O E:GLU190 4.6 11.8 1.0
CA E:SER198 4.6 43.7 1.0
CA E:PRO195 4.6 30.5 1.0
N E:ASP200 4.6 15.1 1.0
CA E:TYR193 4.6 16.2 1.0
CD2 E:TYR193 4.7 22.3 1.0
CB E:ASP200 4.7 29.2 1.0
CB E:TYR193 4.7 32.4 1.0
C E:ASP200 4.7 18.0 1.0
CG2 E:THR194 4.7 15.0 1.0
CG2 E:ILE197 4.8 20.5 1.0
C E:PRO195 4.8 77.1 1.0
C E:SER198 4.9 43.1 1.0
CA E:ASP200 4.9 18.8 1.0
CG E:TYR193 5.0 23.6 1.0

Reference:

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
Page generated: Mon Jul 7 16:53:32 2025

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