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Caesium in PDB 6y4i: Structural and Kinetic Evaluation of Phosphoramidate Inhibitors on Thermolysin

Enzymatic activity of Structural and Kinetic Evaluation of Phosphoramidate Inhibitors on Thermolysin

All present enzymatic activity of Structural and Kinetic Evaluation of Phosphoramidate Inhibitors on Thermolysin:
3.4.24.27;

Protein crystallography data

The structure of Structural and Kinetic Evaluation of Phosphoramidate Inhibitors on Thermolysin, PDB code: 6y4i was solved by M.Kljajic, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.31 / 1.16
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 92.612, 92.612, 129.969, 90, 90, 120
R / Rfree (%) 12.6 / 14

Other elements in 6y4i:

The structure of Structural and Kinetic Evaluation of Phosphoramidate Inhibitors on Thermolysin also contains other interesting chemical elements:

Zinc (Zn) 1 atom
Calcium (Ca) 4 atoms

Caesium Binding Sites:

The binding sites of Caesium atom in the Structural and Kinetic Evaluation of Phosphoramidate Inhibitors on Thermolysin (pdb code 6y4i). This binding sites where shown within 5.0 Angstroms radius around Caesium atom.
In total only one binding site of Caesium was determined in the Structural and Kinetic Evaluation of Phosphoramidate Inhibitors on Thermolysin, PDB code: 6y4i:

Caesium binding site 1 out of 1 in 6y4i

Go back to Caesium Binding Sites List in 6y4i
Caesium binding site 1 out of 1 in the Structural and Kinetic Evaluation of Phosphoramidate Inhibitors on Thermolysin


Mono view


Stereo pair view

A full contact list of Caesium with other atoms in the Cs binding site number 1 of Structural and Kinetic Evaluation of Phosphoramidate Inhibitors on Thermolysin within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cs411

b:16.9
occ:0.46
 O E:SER201 3.0 11.8 0.3
O E:SER201 3.0 12.3 0.7
HB3 E:TYR211 3.2 30.5 1.0
O E:LEU202 3.3 11.4 1.0
OH E:TYR193 3.3 17.8 1.0
HA E:LEU202 3.3 12.7 1.0
CD1 E:TYR211 3.4 25.9 1.0
HD1 E:TYR211 3.4 31.1 1.0
HE2 E:TYR193 3.4 17.2 1.0
CG E:TYR211 3.5 25.3 1.0
CZ E:TYR193 3.8 15.5 1.0
CE2 E:TYR193 3.8 14.4 1.0
CE1 E:TYR211 3.9 26.2 1.0
CB E:TYR211 3.9 25.4 1.0
C E:LEU202 3.9 10.5 1.0
CA E:LEU202 4.0 10.6 1.0
HD12 E:LEU202 4.1 14.7 1.0
C E:SER201 4.1 11.5 0.3
C E:SER201 4.1 11.5 0.7
CD2 E:TYR211 4.1 25.6 1.0
HE1 E:TYR211 4.2 31.5 1.0
O E:HOH713 4.4 16.5 1.0
HB2 E:TYR211 4.4 30.5 1.0
CZ E:TYR211 4.4 27.6 1.0
CE2 E:TYR211 4.5 27.2 1.0
N E:LEU202 4.6 11.0 1.0
HD2 E:TYR211 4.6 30.8 1.0
H E:SER201 4.6 15.3 0.7
H E:SER201 4.7 15.0 0.3
CE1 E:TYR193 4.9 15.1 1.0
CD2 E:TYR193 4.9 13.5 1.0
HA E:TYR211 4.9 30.3 1.0

Reference:

M.Kljajic, H.-D.Gerber, A.Heine, G.Klebe. Structural and Kinetic Evaluation of Phosphoramidate Inhibitors on Thermolysin To Be Published.
Page generated: Sun Jul 13 23:04:00 2025

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