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Calcium in PDB 1b9t: Novel Aromatic Inhibitors of Influenza Virus Neuraminidase Make Selective Interactions with Conserved Residues and Water Molecules in the Active Site

Enzymatic activity of Novel Aromatic Inhibitors of Influenza Virus Neuraminidase Make Selective Interactions with Conserved Residues and Water Molecules in the Active Site

All present enzymatic activity of Novel Aromatic Inhibitors of Influenza Virus Neuraminidase Make Selective Interactions with Conserved Residues and Water Molecules in the Active Site:
3.2.1.18;

Protein crystallography data

The structure of Novel Aromatic Inhibitors of Influenza Virus Neuraminidase Make Selective Interactions with Conserved Residues and Water Molecules in the Active Site, PDB code: 1b9t was solved by J.B.Finley, V.R.Atigadda, F.Duarte, J.J.Zhao, W.J.Brouillette, G.M.Air, M.Luo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.40
Space group P 4 21 2
Cell size a, b, c (Å), α, β, γ (°) 124.500, 124.500, 71.412, 90.00, 90.00, 90.00
R / Rfree (%) 19.5 / 27.1

Calcium Binding Sites:

The binding sites of Calcium atom in the Novel Aromatic Inhibitors of Influenza Virus Neuraminidase Make Selective Interactions with Conserved Residues and Water Molecules in the Active Site (pdb code 1b9t). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Novel Aromatic Inhibitors of Influenza Virus Neuraminidase Make Selective Interactions with Conserved Residues and Water Molecules in the Active Site, PDB code: 1b9t:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1b9t

Go back to Calcium Binding Sites List in 1b9t
Calcium binding site 1 out of 2 in the Novel Aromatic Inhibitors of Influenza Virus Neuraminidase Make Selective Interactions with Conserved Residues and Water Molecules in the Active Site


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Novel Aromatic Inhibitors of Influenza Virus Neuraminidase Make Selective Interactions with Conserved Residues and Water Molecules in the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca500

b:8.2
occ:1.00
O A:ASP293 2.2 13.3 1.0
O A:HOH502 2.2 2.3 1.0
OD2 A:ASP324 2.3 2.0 1.0
O A:GLY346 2.4 19.5 1.0
O A:HOH503 2.4 33.7 1.0
O A:THR297 2.7 12.3 1.0
C A:ASP293 3.4 11.3 1.0
CG A:ASP324 3.4 2.2 1.0
C A:GLY346 3.6 16.4 1.0
C A:THR297 3.8 16.1 1.0
O A:HOH793 3.9 15.2 1.0
CA A:GLY347 3.9 14.7 1.0
O A:TRP344 4.2 20.6 1.0
OD1 A:ASP324 4.2 8.4 1.0
N A:GLY347 4.2 18.0 1.0
CA A:ALA298 4.3 11.3 1.0
N A:ASN294 4.3 12.5 1.0
CA A:ASN294 4.3 15.4 1.0
CB A:ASP324 4.3 2.0 1.0
CA A:ASP293 4.4 8.6 1.0
N A:ALA298 4.4 15.5 1.0
N A:ASP293 4.5 14.4 1.0
CB A:ASP293 4.5 8.2 1.0
N A:GLY346 4.5 21.4 1.0
C A:ASN294 4.5 8.9 1.0
O A:LYS343 4.7 15.5 1.0
CA A:GLY346 4.7 16.5 1.0
N A:THR297 4.7 17.0 1.0
CA A:THR297 4.8 7.8 1.0
N A:SER295 4.9 10.9 1.0
O A:ASN294 4.9 11.7 1.0

Calcium binding site 2 out of 2 in 1b9t

Go back to Calcium Binding Sites List in 1b9t
Calcium binding site 2 out of 2 in the Novel Aromatic Inhibitors of Influenza Virus Neuraminidase Make Selective Interactions with Conserved Residues and Water Molecules in the Active Site


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Novel Aromatic Inhibitors of Influenza Virus Neuraminidase Make Selective Interactions with Conserved Residues and Water Molecules in the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca501

b:20.1
occ:1.00
OE1 A:GLU168 2.7 17.6 1.0
CD A:GLU168 3.9 5.7 1.0
OE2 A:GLU168 4.5 2.0 1.0
O A:HOH668 4.8 5.8 1.0
O A:HOH609 4.8 18.6 1.0
O A:HOH611 5.0 6.0 1.0

Reference:

J.B.Finley, V.R.Atigadda, F.Duarte, J.J.Zhao, W.J.Brouillette, G.M.Air, M.Luo. Novel Aromatic Inhibitors of Influenza Virus Neuraminidase Make Selective Interactions with Conserved Residues and Water Molecules in the Active Site. J.Mol.Biol. V. 293 1107 1999.
ISSN: ISSN 0022-2836
PubMed: 10547289
DOI: 10.1006/JMBI.1999.3180
Page generated: Thu Jul 11 06:19:09 2024

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