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Potassium in PDB 1dil: Sialidase From Salmonella Typhimurium Complexed with Apana and Epana Inhibitors

Enzymatic activity of Sialidase From Salmonella Typhimurium Complexed with Apana and Epana Inhibitors

All present enzymatic activity of Sialidase From Salmonella Typhimurium Complexed with Apana and Epana Inhibitors:
3.2.1.18;

Protein crystallography data

The structure of Sialidase From Salmonella Typhimurium Complexed with Apana and Epana Inhibitors, PDB code: 1dil was solved by E.F.Garman, S.C.Crennell, E.R.Vimr, W.G.Laver, G.L.Taylor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.400, 82.300, 91.700, 90.00, 90.00, 90.00
R / Rfree (%) 18.7 / n/a

Potassium Binding Sites:

The binding sites of Potassium atom in the Sialidase From Salmonella Typhimurium Complexed with Apana and Epana Inhibitors (pdb code 1dil). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Sialidase From Salmonella Typhimurium Complexed with Apana and Epana Inhibitors, PDB code: 1dil:

Potassium binding site 1 out of 1 in 1dil

Go back to Potassium Binding Sites List in 1dil
Potassium binding site 1 out of 1 in the Sialidase From Salmonella Typhimurium Complexed with Apana and Epana Inhibitors


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Sialidase From Salmonella Typhimurium Complexed with Apana and Epana Inhibitors within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K690

b:10.2
occ:1.00
O7 A:AXP384 2.6 8.8 0.6
O6 A:EQP383 2.7 7.7 0.4
OD2 A:ASP62 2.7 10.4 1.0
O7 A:EQP383 2.8 8.1 0.4
O A:HOH697 2.8 27.4 1.0
O3P A:AXP384 2.8 7.0 0.6
O2P A:EQP383 3.0 8.0 0.4
O6 A:AXP384 3.2 9.2 0.6
O A:HOH691 3.4 11.4 1.0
O A:HOH692 3.4 14.5 1.0
C2 A:AXP384 3.4 8.1 0.6
C7 A:EQP383 3.5 8.4 0.4
C7 A:AXP384 3.5 9.0 0.6
C6 A:EQP383 3.6 8.3 0.4
C2 A:EQP383 3.7 7.6 0.4
C8 A:EQP383 3.7 9.6 0.4
P1 A:AXP384 3.8 7.5 0.6
C8 A:AXP384 3.8 9.6 0.6
C6 A:AXP384 3.8 8.8 0.6
O A:HOH693 3.9 12.0 1.0
P1 A:EQP383 3.9 8.5 0.4
CG A:ASP62 4.0 9.7 1.0
O1P A:AXP384 4.1 7.2 0.6
C5 A:EQP383 4.2 8.1 0.4
O3P A:EQP383 4.2 9.5 0.4
C5 A:AXP384 4.2 8.5 0.6
C3 A:EQP383 4.3 6.9 0.4
C9 A:AXP384 4.3 9.9 0.6
C9 A:EQP383 4.5 9.9 0.4
OD1 A:ASP62 4.6 8.3 1.0
C3 A:AXP384 4.7 8.3 0.6
O A:HOH665 4.7 24.0 1.0
OG1 A:THR127 4.7 13.9 1.0
O10 A:AXP384 4.7 9.3 0.6
O8 A:EQP383 4.9 8.9 0.4
O10 A:EQP383 4.9 9.2 0.4
C4 A:EQP383 5.0 7.8 0.4

Reference:

S.J.Crennell, E.F.Garman, C.Philippon, A.Vasella, W.G.Laver, E.R.Vimr, G.L.Taylor. The Structures of Salmonella Typhimurium LT2 Neuraminidase and Its Complexes with Three Inhibitors at High Resolution. J.Mol.Biol. V. 259 264 1996.
ISSN: ISSN 0022-2836
PubMed: 8656428
DOI: 10.1006/JMBI.1996.0318
Page generated: Sun Dec 13 22:42:37 2020

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