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Sodium in PDB 6hdg: D170N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed with Beta-G1P in A Closed Conformer to 1.2 A.

Enzymatic activity of D170N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed with Beta-G1P in A Closed Conformer to 1.2 A.

All present enzymatic activity of D170N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed with Beta-G1P in A Closed Conformer to 1.2 A.:
5.4.2.6;

Protein crystallography data

The structure of D170N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed with Beta-G1P in A Closed Conformer to 1.2 A., PDB code: 6hdg was solved by H.P.Wood, A.J.Robertson, C.Bisson, J.P.Waltho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.86 / 1.15
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 37.560, 55.080, 105.840, 90.00, 90.00, 90.00
R / Rfree (%) 15 / 17.6

Sodium Binding Sites:

The binding sites of Sodium atom in the D170N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed with Beta-G1P in A Closed Conformer to 1.2 A. (pdb code 6hdg). 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 D170N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed with Beta-G1P in A Closed Conformer to 1.2 A., PDB code: 6hdg:

Sodium binding site 1 out of 1 in 6hdg

Go back to Sodium Binding Sites List in 6hdg
Sodium binding site 1 out of 1 in the D170N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed with Beta-G1P in A Closed Conformer to 1.2 A.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of D170N Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed with Beta-G1P in A Closed Conformer to 1.2 A. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na306

b:13.4
occ:1.00
 O A:GLU124 2.3 11.4 1.0
OD1 A:ASN127 2.4 13.1 1.0
O A:HOH582 2.5 20.2 1.0
O A:HOH571 2.5 34.3 1.0
O A:HOH474 2.5 15.1 1.0
C A:GLU124 3.4 10.5 1.0
CG A:ASN127 3.5 11.8 1.0
ND2 A:ASN127 4.1 15.2 1.0
O A:ARG125 4.2 9.8 1.0
C A:ARG125 4.2 9.4 1.0
N A:ARG125 4.2 9.7 1.0
CA A:ARG125 4.2 9.6 1.0
N A:ASN127 4.3 9.0 1.0
CA A:GLU124 4.4 10.5 1.0
CA A:ASN127 4.4 10.4 1.0
CB A:ASN127 4.6 11.3 1.0
NH1 A:ARG125 4.8 13.5 1.0
CB A:GLU124 4.8 13.7 1.0
O A:HOH598 5.0 28.9 1.0
N A:MET126 5.0 9.2 1.0
OE2 A:GLU124 5.0 33.7 1.0

Reference:

A.J.Robertson, C.Bisson, J.P.Waltho. Transition State of Phospho-Enzyme Hydrolysis in Beta-Phosphoglucomutase. To Be Published.
Page generated: Tue Oct 8 09:17:28 2024

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