Zinc in PDB 1lnd: 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: 1lnd 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 (°)	93.852, 93.852, 131.322, 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)

4 atoms

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

Zinc 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 Zinc with other atoms in the Zn 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:Zn800 b:14.9 occ:1.00 O E:HOH910 1.8 21.4 1.0 NE2 E:HIS142 1.9 14.1 1.0 NE2 E:HIS146 2.0 10.5 1.0 OE1 E:GLU166 2.1 18.8 1.0 OE2 E:GLU166 2.7 33.0 1.0 CD E:GLU166 2.7 14.3 1.0 CE1 E:HIS142 2.9 17.1 1.0 CE1 E:HIS146 3.0 17.4 1.0 CD2 E:HIS142 3.0 20.2 1.0 CD2 E:HIS146 3.0 15.5 1.0 ZN E:ZN801 3.2 30.6 0.5 OE2 E:GLU143 3.6 16.3 0.5 ND1 E:HIS142 4.1 10.6 1.0 CG E:HIS142 4.1 10.5 1.0 ND1 E:HIS146 4.1 15.6 1.0 CG E:HIS146 4.1 12.0 1.0 CG E:GLU166 4.2 11.9 1.0 OH E:TYR157 4.2 46.9 1.0 NE2 E:HIS231 4.2 26.0 1.0 O E:HOH1058 4.2 37.9 1.0 CA E:VAL1321 4.3 47.1 1.0 CD E:GLU143 4.4 81.5 0.5 OE1 E:GLU143 4.4 12.7 0.5 OE1 E:GLU143 4.4 8.4 0.5 CB E:SER169 4.5 9.8 1.0 O E:VAL1321 4.7 32.5 1.0 C E:VAL1321 4.7 78.5 1.0 OG E:SER169 4.7 11.7 1.0 N E:VAL1321 4.7 37.9 1.0 CA E:GLU166 4.7 13.5 1.0 CD2 E:HIS231 4.8 30.0 1.0 CB E:GLU166 4.8 13.6 1.0 CE1 E:TYR157 4.9 0.0 1.0 CZ E:TYR157 5.0 0.0 1.0

Zinc 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 Zinc with other atoms in the Zn 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:Zn801 b:30.6 occ:0.50 OH E:TYR157 1.8 46.9 1.0 O E:HOH910 2.0 21.4 1.0 NE2 E:HIS231 2.3 26.0 1.0 OE2 E:GLU166 2.6 33.0 1.0 CE1 E:HIS231 2.7 20.0 1.0 CZ E:TYR157 3.1 0.0 1.0 ZN E:ZN800 3.2 14.9 1.0 CD E:GLU166 3.4 14.3 1.0 CD2 E:HIS231 3.6 30.0 1.0 OE1 E:GLU166 3.6 18.8 1.0 CE1 E:TYR157 3.8 0.0 1.0 ND1 E:HIS231 4.0 32.6 1.0 O E:HOH1058 4.1 37.9 1.0 CE2 E:TYR157 4.2 0.0 1.0 N E:LYS1322 4.3 61.1 1.0 C E:VAL1321 4.3 78.5 1.0 N E:VAL1321 4.3 37.9 1.0 NE2 E:HIS146 4.4 10.5 1.0 CG E:HIS231 4.4 21.6 1.0 O E:LYS1322 4.4 52.8 1.0 CG E:GLU166 4.5 11.9 1.0 CA E:VAL1321 4.5 47.1 1.0 O E:VAL1321 4.6 32.5 1.0 CA E:LYS1322 4.8 76.2 1.0 NE2 E:HIS142 4.8 14.1 1.0 C E:LYS1322 4.9 0.0 1.0 OE2 E:GLU143 5.0 16.3 0.5

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