Manganese in PDB 1lnc: 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: 1lnc 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 / 1.80
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	93.900, 93.900, 131.200, 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:

Calcium

(Ca)

2 atoms

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

Manganese 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 Manganese with other atoms in the Mn 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:Mn900 b:11.9 occ:1.00 NE2 E:HIS142 2.1 12.2 1.0 OE2 E:GLU166 2.1 14.4 1.0 NE2 E:HIS146 2.1 10.7 1.0 O E:HOH907 2.2 26.1 1.0 O E:HOH906 2.3 33.1 1.0 CD E:GLU166 2.8 18.6 1.0 OE1 E:GLU166 3.0 21.2 1.0 CE1 E:HIS142 3.1 11.2 1.0 CD2 E:HIS142 3.1 21.6 1.0 CD2 E:HIS146 3.1 15.6 1.0 CE1 E:HIS146 3.1 15.1 1.0 OE1 E:GLU143 3.6 33.0 0.3 OH E:TYR157 3.7 26.3 1.0 ND1 E:HIS146 4.2 14.2 1.0 NE2 E:HIS231 4.2 20.1 1.0 CG E:HIS142 4.2 10.8 1.0 ND1 E:HIS142 4.2 9.3 1.0 CG E:HIS146 4.2 8.8 1.0 OE2 E:GLU143 4.3 8.4 0.3 CG E:GLU166 4.3 11.2 1.0 CA E:VAL1321 4.3 54.2 1.0 OE1 E:GLU143 4.3 21.4 0.7 CD E:GLU143 4.4 3.0 0.3 O E:HOH939 4.4 27.4 1.0 N E:VAL1321 4.5 31.4 1.0 O E:HOH389 4.6 50.5 1.0 CB E:SER169 4.7 9.0 1.0 O E:VAL1321 4.7 33.6 1.0 C E:VAL1321 4.7 0.0 1.0 CZ E:TYR157 4.8 30.7 1.0 OG E:SER169 4.9 11.3 1.0 CD2 E:HIS231 4.9 18.1 1.0 CA E:GLU166 4.9 12.3 1.0

Manganese 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 Manganese with other atoms in the Mn 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:Mn902 b:14.8 occ:1.00 OE2 E:GLU177 2.0 15.7 1.0 OE2 E:GLU190 2.0 17.1 1.0 OD2 E:ASP185 2.0 16.5 1.0 O E:HOH909 2.1 16.1 1.0 O E:ASN183 2.2 19.9 1.0 O E:HOH905 2.2 15.1 1.0 CG E:ASP185 3.0 16.2 1.0 CD E:GLU177 3.1 18.8 1.0 CD E:GLU190 3.1 17.1 1.0 C E:ASN183 3.4 12.3 1.0 OD1 E:ASP185 3.5 12.8 1.0 CA E:CA901 3.6 13.1 1.0 CG E:GLU190 3.6 12.3 1.0 OE1 E:GLU177 3.7 16.4 1.0 O E:LYS182 3.9 22.0 1.0 O E:HOH1068 4.0 72.9 1.0 CA E:PRO184 4.1 15.8 1.0 CG E:GLU177 4.1 11.9 1.0 N E:ASP185 4.1 16.1 1.0 OE1 E:GLU190 4.1 12.9 1.0 C E:PRO184 4.1 24.5 1.0 CB E:ASN183 4.1 26.0 1.0 OD2 E:ASP191 4.2 15.6 1.0 N E:PRO184 4.2 20.4 1.0 OD1 E:ASP191 4.2 16.9 1.0 CB E:ASP185 4.3 19.1 1.0 CA E:ASN183 4.5 14.6 1.0 CG E:ASP191 4.5 21.6 1.0 O E:PRO184 4.8 21.9 1.0 CA E:ASP185 4.8 11.7 1.0 O E:HOH982 4.9 66.1 1.0

Manganese 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 Manganese with other atoms in the Mn 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:Mn903 b:16.1 occ:1.00 O E:HOH911 2.1 16.3 1.0 OD1 E:ASP57 2.1 16.5 1.0 O E:GLN61 2.2 14.0 1.0 OD1 E:ASP59 2.2 19.8 1.0 O E:HOH908 2.2 15.9 1.0 O E:HOH912 2.3 15.7 1.0 CG E:ASP57 2.9 15.0 1.0 OD2 E:ASP57 3.0 17.1 1.0 CG E:ASP59 3.2 24.0 1.0 C E:GLN61 3.4 26.7 1.0 OD2 E:ASP59 3.5 19.3 1.0 O E:HOH990 3.9 27.3 1.0 N E:GLN61 4.0 11.6 1.0 CA E:GLN61 4.1 12.1 1.0 N E:ASP59 4.3 14.3 1.0 CB E:GLN61 4.3 14.2 1.0 O E:HOH1045 4.3 53.8 1.0 CB E:ASP57 4.4 8.7 1.0 N E:PHE62 4.4 14.4 1.0 O E:HOH935 4.4 15.7 1.0 O E:HOH1001 4.5 18.4 1.0 CB E:ASP59 4.5 13.3 1.0 OD2 E:ASP67 4.5 12.2 1.0 O E:HOH1060 4.5 44.5 1.0 CA E:PHE62 4.6 13.7 1.0 O E:HOH1064 4.6 58.2 1.0 N E:ALA58 4.7 10.6 1.0 N E:ASN60 4.8 14.9 1.0 CA E:ASP59 4.8 10.6 1.0 C E:ASP59 5.0 16.4 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