Cobalt in PDB 1lna: 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: 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

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

Calcium

(Ca)

3 atoms

The binding sites of Cobalt 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 Cobalt atom.
In total 2 binding sites of Cobalt where determined in the A Structural Analysis of Metal Substitutions in Thermolysin, PDB code: 1lna:
Jump to Cobalt binding site number: 1; 2;

Cobalt 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 Cobalt with other atoms in the Co 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:Co900 b:14.7 occ:1.00 NE2 E:HIS142 2.0 12.5 1.0 NE2 E:HIS146 2.1 10.8 1.0 O E:HOH907 2.2 28.3 1.0 OE1 E:GLU166 2.3 16.7 1.0 OE2 E:GLU166 2.3 36.3 1.0 O E:HOH906 2.4 12.9 1.0 CD E:GLU166 2.6 11.7 1.0 CE1 E:HIS142 2.9 10.8 1.0 CD2 E:HIS146 3.0 12.2 1.0 CE1 E:HIS146 3.1 13.6 1.0 CD2 E:HIS142 3.1 18.7 1.0 OH E:TYR157 4.0 53.8 1.0 NE2 E:HIS231 4.1 17.0 1.0 CA E:VAL1321 4.1 34.6 1.0 N E:VAL1321 4.1 23.6 1.0 ND1 E:HIS142 4.1 8.3 1.0 CG E:GLU166 4.1 6.8 1.0 CG E:HIS146 4.2 5.5 1.0 ND1 E:HIS146 4.2 10.2 1.0 CG E:HIS142 4.2 6.0 1.0 OE1 E:GLU143 4.3 13.3 1.0 O E:HOH938 4.4 23.5 1.0 C E:VAL1321 4.5 0.0 1.0 CB E:SER169 4.7 3.5 1.0 O E:VAL1321 4.7 26.6 1.0 CB E:GLU166 4.8 12.9 1.0 CD2 E:HIS231 4.8 19.6 1.0 CA E:GLU166 4.8 5.7 1.0 OG E:SER169 4.9 11.2 1.0 CZ E:TYR157 5.0 38.7 1.0 CE1 E:TYR157 5.0 0.0 1.0

Cobalt 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 Cobalt with other atoms in the Co 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:Co903 b:13.9 occ:1.00 O E:HOH910 2.1 12.7 1.0 OD1 E:ASP57 2.1 12.7 1.0 OD1 E:ASP59 2.2 14.3 1.0 O E:GLN61 2.2 11.4 1.0 O E:HOH911 2.2 14.8 1.0 O E:HOH908 2.3 13.2 1.0 CG E:ASP57 3.0 16.0 1.0 CG E:ASP59 3.1 17.9 1.0 OD2 E:ASP57 3.2 15.4 1.0 OD2 E:ASP59 3.4 17.5 1.0 C E:GLN61 3.4 22.1 1.0 N E:GLN61 3.9 8.6 1.0 O E:HOH991 4.0 27.6 1.0 CA E:GLN61 4.1 16.4 1.0 O E:HOH1061 4.2 47.2 1.0 O E:HOH1046 4.2 37.7 1.0 O E:HOH934 4.2 12.2 1.0 CB E:GLN61 4.3 9.6 1.0 N E:ASP59 4.3 9.2 1.0 CB E:ASP57 4.4 5.8 1.0 N E:PHE62 4.4 9.0 1.0 O E:HOH1002 4.4 13.2 1.0 OD2 E:ASP67 4.5 10.7 1.0 CB E:ASP59 4.5 6.8 1.0 CA E:PHE62 4.5 8.6 1.0 N E:ALA58 4.6 6.5 1.0 CA E:ASP59 4.8 7.6 1.0 N E:ASN60 4.8 11.8 1.0 C E:ASP59 5.0 6.5 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