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Calcium in PDB 1mwe: The X-Ray Structure of A Complex of Tern N9 Influenza Virus Neuraminidase Complexed with Sialic Acid at 4 Degrees C Revealing A Second Sialic Acid Binding Site

Enzymatic activity of The X-Ray Structure of A Complex of Tern N9 Influenza Virus Neuraminidase Complexed with Sialic Acid at 4 Degrees C Revealing A Second Sialic Acid Binding Site

All present enzymatic activity of The X-Ray Structure of A Complex of Tern N9 Influenza Virus Neuraminidase Complexed with Sialic Acid at 4 Degrees C Revealing A Second Sialic Acid Binding Site:
3.2.1.18;

Protein crystallography data

The structure of The X-Ray Structure of A Complex of Tern N9 Influenza Virus Neuraminidase Complexed with Sialic Acid at 4 Degrees C Revealing A Second Sialic Acid Binding Site, PDB code: 1mwe was solved by J.N.Varghese, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 1.70
Space group I 4 3 2
Cell size a, b, c (Å), α, β, γ (°) 181.040, 181.040, 181.040, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the The X-Ray Structure of A Complex of Tern N9 Influenza Virus Neuraminidase Complexed with Sialic Acid at 4 Degrees C Revealing A Second Sialic Acid Binding Site (pdb code 1mwe). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the The X-Ray Structure of A Complex of Tern N9 Influenza Virus Neuraminidase Complexed with Sialic Acid at 4 Degrees C Revealing A Second Sialic Acid Binding Site, PDB code: 1mwe:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1mwe

Go back to Calcium Binding Sites List in 1mwe
Calcium binding site 1 out of 2 in the The X-Ray Structure of A Complex of Tern N9 Influenza Virus Neuraminidase Complexed with Sialic Acid at 4 Degrees C Revealing A Second Sialic Acid Binding Site


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The X-Ray Structure of A Complex of Tern N9 Influenza Virus Neuraminidase Complexed with Sialic Acid at 4 Degrees C Revealing A Second Sialic Acid Binding Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca999

b:15.2
occ:1.00
O A:GLY297 2.5 15.0 1.0
O A:ASP293 2.5 12.4 1.0
O A:ASN347 2.7 15.4 1.0
O A:HOH1007 2.7 13.1 1.0
O A:HOH1088 2.7 15.0 1.0
OD2 A:ASP324 2.8 11.6 1.0
C A:GLY297 3.6 15.3 1.0
CG A:ASP324 3.6 11.1 1.0
C A:ASP293 3.6 11.8 1.0
C A:ASN347 3.8 15.2 1.0
O A:ASN294 3.9 12.6 1.0
CA A:GLY348 4.0 13.3 1.0
CA A:ASN294 4.0 12.6 1.0
O A:HOH1213 4.0 21.6 1.0
O A:HOH1006 4.1 8.7 1.0
C A:ASN294 4.2 13.2 1.0
CB A:ASP324 4.2 11.6 1.0
N A:ASN294 4.3 11.8 1.0
N A:GLY297 4.3 16.7 1.0
OD1 A:ASP324 4.4 11.2 1.0
N A:GLY348 4.4 14.1 1.0
CA A:GLY297 4.4 15.8 1.0
N A:SER298 4.5 14.8 1.0
CA A:SER298 4.7 14.8 1.0
CA A:ASP293 4.7 12.0 1.0
N A:ASP293 4.8 11.8 1.0
C A:GLN296 4.8 16.8 1.0
N A:ASN347 4.9 16.0 1.0
O A:ASN344 4.9 18.4 1.0
CB A:ASP293 4.9 12.4 1.0

Calcium binding site 2 out of 2 in 1mwe

Go back to Calcium Binding Sites List in 1mwe
Calcium binding site 2 out of 2 in the The X-Ray Structure of A Complex of Tern N9 Influenza Virus Neuraminidase Complexed with Sialic Acid at 4 Degrees C Revealing A Second Sialic Acid Binding Site


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of The X-Ray Structure of A Complex of Tern N9 Influenza Virus Neuraminidase Complexed with Sialic Acid at 4 Degrees C Revealing A Second Sialic Acid Binding Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca998

b:6.9
occ:0.25
O A:HOH1299 2.9 20.6 1.0
O A:HOH1053 3.6 24.6 1.0
OD1 A:ASP113 4.9 11.2 1.0
OD2 A:ASP113 4.9 11.3 1.0

Reference:

J.N.Varghese, P.M.Colman, A.Van Donkelaar, T.J.Blick, A.Sahasrabudhe, J.L.Mckimm-Breschkin. Structural Evidence For A Second Sialic Acid Binding Site in Avian Influenza Virus Neuraminidases. Proc.Natl.Acad.Sci.Usa V. 94 11808 1997.
ISSN: ISSN 0027-8424
PubMed: 9342319
DOI: 10.1073/PNAS.94.22.11808
Page generated: Thu Jul 11 12:37:59 2024

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