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Sodium in PDB 1ns4: Crystal Structure of Galactose Mutarotase From Lactococcus Lactis Mutant E304Q Complexed with Glucose

Enzymatic activity of Crystal Structure of Galactose Mutarotase From Lactococcus Lactis Mutant E304Q Complexed with Glucose

All present enzymatic activity of Crystal Structure of Galactose Mutarotase From Lactococcus Lactis Mutant E304Q Complexed with Glucose:
5.1.3.3;

Protein crystallography data

The structure of Crystal Structure of Galactose Mutarotase From Lactococcus Lactis Mutant E304Q Complexed with Glucose, PDB code: 1ns4 was solved by H.M.Holden, J.B.Thoden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.85
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.800, 76.200, 210.700, 90.00, 90.00, 90.00
R / Rfree (%) 15.7 / 21.6

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Galactose Mutarotase From Lactococcus Lactis Mutant E304Q Complexed with Glucose (pdb code 1ns4). 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 of Galactose Mutarotase From Lactococcus Lactis Mutant E304Q Complexed with Glucose, PDB code: 1ns4:

Sodium binding site 1 out of 1 in 1ns4

Go back to Sodium Binding Sites List in 1ns4
Sodium binding site 1 out of 1 in the Crystal Structure of Galactose Mutarotase From Lactococcus Lactis Mutant E304Q Complexed with Glucose


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Galactose Mutarotase From Lactococcus Lactis Mutant E304Q Complexed with Glucose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1401

b:41.1
occ:1.00
 O A:HOH1640 2.5 27.8 1.0
OD1 A:ASP13 2.5 22.8 1.0
O A:GLY11 2.5 22.8 1.0
OD2 B:ASP13 2.5 18.8 1.0
OD1 B:ASP13 2.5 20.8 1.0
CG B:ASP13 2.8 21.6 1.0
C A:GLY11 3.3 22.2 1.0
CG A:ASP13 3.5 21.8 1.0
O A:HOH1413 3.6 20.1 1.0
O A:SER12 3.8 19.0 1.0
CA A:GLY11 3.9 18.1 1.0
C A:SER12 3.9 24.0 1.0
O B:GLY11 4.0 21.1 1.0
OD2 A:ASP13 4.0 23.5 1.0
O B:HOH2550 4.1 28.3 1.0
N A:SER12 4.2 21.4 1.0
CB B:ASP13 4.2 20.3 1.0
N A:ASP13 4.3 16.1 1.0
CA A:SER12 4.4 19.7 1.0
CB A:ASP13 4.6 15.2 1.0
CA A:ASP13 4.6 13.4 1.0
OD1 A:ASP7 4.8 0.0 1.0
OH B:TYR109 4.9 19.2 1.0
N B:ASP13 4.9 18.8 1.0
CA B:ASP13 5.0 20.3 1.0
C B:GLY11 5.0 25.5 1.0

Reference:

J.B.Thoden, J.Kim, F.M.Raushel, H.M.Holden. The Catalytic Mechanism of Galactose Mutarotase Protein Sci. V. 12 1051 2003.
ISSN: ISSN 0961-8368
PubMed: 12717027
DOI: 10.1110/PS.0243203
Page generated: Sun Aug 17 06:44:24 2025

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