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Zinc in PDB 5dlh: Sfx Structure of Thermolysin

Enzymatic activity of Sfx Structure of Thermolysin

All present enzymatic activity of Sfx Structure of Thermolysin:
3.4.24.27;

Protein crystallography data

The structure of Sfx Structure of Thermolysin, PDB code: 5dlh was solved by H.D.Demirci, N.K.Sauter, A.S.Brewster, J.Kern, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.20 / 2.25
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.794, 93.794, 132.243, 90.00, 90.00, 120.00
R / Rfree (%) 17.9 / 22.7

Other elements in 5dlh:

The structure of Sfx Structure of Thermolysin also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Sfx Structure of Thermolysin (pdb code 5dlh). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Sfx Structure of Thermolysin, PDB code: 5dlh:

Zinc binding site 1 out of 1 in 5dlh

Go back to Zinc Binding Sites List in 5dlh
Zinc binding site 1 out of 1 in the Sfx Structure of Thermolysin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Sfx Structure of Thermolysin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:41.7
occ:1.00
NE2 A:HIS146 2.1 43.5 1.0
NE2 A:HIS142 2.2 34.3 1.0
OE2 A:GLU166 2.3 44.7 1.0
O A:HOH568 2.4 42.0 1.0
OE1 A:GLU166 2.5 43.8 1.0
O A:HOH501 2.6 41.9 1.0
CD A:GLU166 2.7 43.9 1.0
CE1 A:HIS146 2.9 41.7 1.0
HE1 A:HIS146 3.0 50.1 1.0
CD2 A:HIS142 3.1 35.4 1.0
CE1 A:HIS142 3.2 33.7 1.0
CD2 A:HIS146 3.2 43.7 1.0
HD2 A:HIS142 3.3 42.5 1.0
HE1 A:HIS142 3.3 40.4 1.0
HD2 A:HIS146 3.5 52.4 1.0
OH A:TYR157 3.9 34.8 0.6
HA A:GLU166 3.9 45.0 1.0
ND1 A:HIS146 4.1 40.8 1.0
NE2 A:HIS231 4.1 45.2 1.0
HB2 A:SER169 4.2 42.8 1.0
CG A:GLU166 4.2 43.2 1.0
ND1 A:HIS142 4.3 34.0 1.0
O A:HOH535 4.3 44.8 1.0
CG A:HIS146 4.3 41.9 1.0
CG A:HIS142 4.3 34.8 1.0
HB3 A:SER169 4.3 42.8 1.0
HH A:TYR157 4.3 41.8 0.6
HE1 A:TYR157 4.3 45.6 0.6
HD2 A:HIS231 4.4 54.2 1.0
O A:HOH504 4.5 38.7 1.0
OE1 A:GLU143 4.5 38.6 1.0
HG2 A:GLU166 4.5 51.9 1.0
CB A:SER169 4.5 35.6 1.0
OG A:SER169 4.6 37.5 1.0
O A:HOH575 4.6 32.3 1.0
CD2 A:HIS231 4.7 45.2 1.0
HG3 A:GLU166 4.7 51.9 1.0
CA A:GLU166 4.8 37.5 1.0
CZ A:TYR157 4.8 36.8 0.6
OE2 A:GLU143 4.8 37.5 1.0
HD1 A:HIS146 4.9 49.0 1.0
CE1 A:TYR157 4.9 38.0 0.6
CB A:GLU166 4.9 39.9 1.0
HB3 A:GLU166 4.9 47.9 1.0
HH22 A:ARG203 4.9 43.4 1.0

Reference:

H.D.Demirci, H.D.Demirci, N.K.Sauter, A.S.Brewster, J.Kern. N/A N/A.
Page generated: Sun Oct 27 14:48:09 2024

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