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Sodium in PDB 1w8o: Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase From Micromonospora Viridifaciens

Enzymatic activity of Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase From Micromonospora Viridifaciens

All present enzymatic activity of Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase From Micromonospora Viridifaciens:
3.2.1.18;

Protein crystallography data

The structure of Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase From Micromonospora Viridifaciens, PDB code: 1w8o was solved by S.Newstead, J.N.Watson, V.Dookhun, A.J.Bennet, G.Taylor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 87.71 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.712, 111.168, 142.195, 90.00, 90.00, 90.00
R / Rfree (%) 16.2 / 19.7

Sodium Binding Sites:

The binding sites of Sodium atom in the Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase From Micromonospora Viridifaciens (pdb code 1w8o). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase From Micromonospora Viridifaciens, PDB code: 1w8o:

Sodium binding site 1 out of 1 in 1w8o

Go back to Sodium Binding Sites List in 1w8o
Sodium binding site 1 out of 1 in the Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase From Micromonospora Viridifaciens


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase From Micromonospora Viridifaciens within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1654

b:11.7
occ:1.00
 O A:ASN528 2.3 22.5 1.0
O A:ASN533 2.3 26.9 1.0
OE2 A:GLU640 2.4 24.3 1.0
O A:ALA639 2.5 19.4 1.0
OD1 A:ASP531 2.5 24.0 1.0
O A:THR536 2.5 20.3 1.0
OG1 A:THR536 2.6 22.7 1.0
C A:THR536 3.4 22.5 1.0
C A:ASN533 3.5 27.3 1.0
C A:ASN528 3.5 22.1 1.0
CG A:ASP531 3.5 25.9 1.0
CD A:GLU640 3.5 25.8 1.0
C A:ALA639 3.6 18.6 1.0
CB A:THR536 3.8 25.8 1.0
OD2 A:ASP531 3.8 27.4 1.0
CA A:THR536 4.0 24.4 1.0
N A:ASN533 4.0 27.2 1.0
N A:THR536 4.0 24.6 1.0
CG A:GLU640 4.1 23.8 1.0
CA A:ASN533 4.2 26.4 1.0
CB A:ASN533 4.3 27.5 1.0
CA A:ASN528 4.3 21.2 1.0
CA A:VAL529 4.4 19.5 1.0
CA A:ALA639 4.4 18.2 1.0
N A:VAL529 4.4 20.6 1.0
N A:PHE537 4.5 21.4 1.0
N A:PRO534 4.5 27.8 1.0
CB A:ASN528 4.5 21.4 1.0
C A:VAL529 4.6 20.1 1.0
OE1 A:GLU640 4.6 29.9 1.0
N A:GLU640 4.6 18.7 1.0
CA A:PRO534 4.7 27.9 1.0
N A:ASP531 4.7 25.2 1.0
CA A:GLU640 4.7 18.7 1.0
CB A:ASP531 4.8 26.6 1.0
N A:GLY532 4.8 27.8 1.0
C A:PRO534 4.8 27.5 1.0
CA A:PHE537 4.8 20.5 1.0
CG2 A:THR536 4.8 27.9 1.0
O A:VAL529 4.9 20.6 1.0
CB A:ALA639 4.9 18.8 1.0
N A:ILE530 5.0 20.9 1.0
CB A:GLU640 5.0 19.3 1.0

Reference:

J.N.Watson, S.Newstead, V.Dookhun, G.Taylor, A.J.Bennet. Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase From Micromonospora Viridifaciens Febs Lett. V. 577 265 2004.
ISSN: ISSN 0014-5793
PubMed: 15527797
DOI: 10.1016/J.FEBSLET.2004.10.016
Page generated: Mon Oct 7 00:24:20 2024

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