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Sodium in PDB 2wnn: Structure of Wild Type E. Coli N-Acetylneuraminic Acid Lyase in Complex with Pyruvate in Space Group P21

Enzymatic activity of Structure of Wild Type E. Coli N-Acetylneuraminic Acid Lyase in Complex with Pyruvate in Space Group P21

All present enzymatic activity of Structure of Wild Type E. Coli N-Acetylneuraminic Acid Lyase in Complex with Pyruvate in Space Group P21:
4.1.3.3;

Protein crystallography data

The structure of Structure of Wild Type E. Coli N-Acetylneuraminic Acid Lyase in Complex with Pyruvate in Space Group P21, PDB code: 2wnn was solved by I.Campeotto, A.H.Bolt, T.A.Harman, C.H.Trinh, C.A.Dennis, S.E.V.Phillips, A.R.Pearson, A.Nelson, A.Berry, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 79.07 / 1.65
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 54.693, 142.456, 83.626, 90.00, 109.16, 90.00
R / Rfree (%) 20.986 / 24.92

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure of Wild Type E. Coli N-Acetylneuraminic Acid Lyase in Complex with Pyruvate in Space Group P21 (pdb code 2wnn). 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 Structure of Wild Type E. Coli N-Acetylneuraminic Acid Lyase in Complex with Pyruvate in Space Group P21, PDB code: 2wnn:

Sodium binding site 1 out of 1 in 2wnn

Go back to Sodium Binding Sites List in 2wnn
Sodium binding site 1 out of 1 in the Structure of Wild Type E. Coli N-Acetylneuraminic Acid Lyase in Complex with Pyruvate in Space Group P21


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of Wild Type E. Coli N-Acetylneuraminic Acid Lyase in Complex with Pyruvate in Space Group P21 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na1297

b:43.4
occ:1.00
O B:VAL265 3.7 27.6 1.0
C B:ASP263 3.8 29.3 1.0
O B:ASP263 3.8 29.3 1.0
C B:VAL265 3.9 27.7 1.0
CA B:ASP263 3.9 29.8 1.0
CA B:SER266 3.9 27.3 1.0
NH1 B:ARG29 4.0 37.3 1.0
N B:SER266 4.1 27.7 1.0
O B:HIS260 4.4 26.2 1.0
N B:VAL264 4.4 28.8 1.0
N B:VAL265 4.4 27.6 1.0
OD1 B:ASP263 4.5 36.3 1.0
OG B:SER266 4.5 27.5 1.0
C B:VAL264 4.6 28.0 1.0
CB B:ASP263 4.7 30.5 1.0
CB B:SER266 4.7 27.2 1.0
CD2 B:HIS260 4.8 28.3 1.0
CA B:VAL265 4.8 27.6 1.0
O B:VAL264 4.9 28.1 1.0
C B:SER266 5.0 27.4 1.0
N B:ASP263 5.0 29.4 1.0
O B:SER266 5.0 27.5 1.0

Reference:

I.Campeotto, A.H.Bolt, T.A.Harman, C.A.Dennis, C.H.Trinh, S.E.V.Phillips, A.Nelson, A.R.Pearson, A.Berry. Structural Insights Into Substrate Specificity in Variants of N-Acetylneuraminic Acid Lyase Produced By Directed Evolution. J.Mol.Biol. V. 404 56 2010.
ISSN: ISSN 0022-2836
PubMed: 20826162
DOI: 10.1016/J.JMB.2010.08.008
Page generated: Mon Oct 7 04:43:20 2024

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