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Sodium in PDB 3lu1: Crystal Structure Analysis of Wbgu: A Udp-Galnac 4-Epimerase

Enzymatic activity of Crystal Structure Analysis of Wbgu: A Udp-Galnac 4-Epimerase

All present enzymatic activity of Crystal Structure Analysis of Wbgu: A Udp-Galnac 4-Epimerase:
5.1.3.7;

Protein crystallography data

The structure of Crystal Structure Analysis of Wbgu: A Udp-Galnac 4-Epimerase, PDB code: 3lu1 was solved by V.S.Bhatt, C.Y.Guo, G.Zhao, W.Yi, Z.J.Liu, P.G.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.03 / 2.50
Space group P 32
Cell size a, b, c (Å), α, β, γ (°) 78.130, 78.130, 231.924, 90.00, 90.00, 120.00
R / Rfree (%) 20.4 / 25.8

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure Analysis of Wbgu: A Udp-Galnac 4-Epimerase (pdb code 3lu1). 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 Crystal Structure Analysis of Wbgu: A Udp-Galnac 4-Epimerase, PDB code: 3lu1:

Sodium binding site 1 out of 1 in 3lu1

Go back to Sodium Binding Sites List in 3lu1
Sodium binding site 1 out of 1 in the Crystal Structure Analysis of Wbgu: A Udp-Galnac 4-Epimerase


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure Analysis of Wbgu: A Udp-Galnac 4-Epimerase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Na345

b:38.9
occ:1.00
O D:HOH382 2.2 48.4 1.0
O D:HOH380 2.4 39.4 1.0
O D:HOH381 2.7 29.3 1.0
CD2 D:TYR5 4.0 34.6 1.0
CE2 D:TYR5 4.1 34.3 1.0
CE D:MET2 4.4 41.6 1.0
CG D:TYR5 4.6 34.2 1.0
CA D:GLU6 4.7 34.0 1.0
NZ D:LYS35 4.7 36.4 1.0
CG D:GLU6 4.7 34.1 1.0
OG1 D:THR9 4.7 35.6 1.0
N D:GLU6 4.8 34.2 1.0
CZ D:TYR5 4.8 33.8 1.0

Reference:

V.S.Bhatt, C.Y.Guo, W.Guan, G.Zhao, W.Yi, Z.J.Liu, P.G.Wang. Altered Architecture of Substrate Binding Region Defines the Unique Specificity of Udp-Galnac 4-Epimerases. Protein Sci. V. 20 856 2011.
ISSN: ISSN 0961-8368
PubMed: 21384454
DOI: 10.1002/PRO.611
Page generated: Tue Dec 15 06:17:02 2020

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