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Sodium in PDB 8uy2: Methylenetetrahydrofolate Reductase From Chaetomium Thermophilum Dsm 1495, Adomet-Bound, Inhibited (T) State

Enzymatic activity of Methylenetetrahydrofolate Reductase From Chaetomium Thermophilum Dsm 1495, Adomet-Bound, Inhibited (T) State

All present enzymatic activity of Methylenetetrahydrofolate Reductase From Chaetomium Thermophilum Dsm 1495, Adomet-Bound, Inhibited (T) State:
1.5.1.20;

Protein crystallography data

The structure of Methylenetetrahydrofolate Reductase From Chaetomium Thermophilum Dsm 1495, Adomet-Bound, Inhibited (T) State, PDB code: 8uy2 was solved by K.Yamada, J.Mendoza, M.Koutmos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 74.97 / 2.83
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 130.656, 149.948, 171.056, 90, 90, 90
R / Rfree (%) 18.7 / 20.3

Sodium Binding Sites:

The binding sites of Sodium atom in the Methylenetetrahydrofolate Reductase From Chaetomium Thermophilum Dsm 1495, Adomet-Bound, Inhibited (T) State (pdb code 8uy2). 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 Methylenetetrahydrofolate Reductase From Chaetomium Thermophilum Dsm 1495, Adomet-Bound, Inhibited (T) State, PDB code: 8uy2:

Sodium binding site 1 out of 1 in 8uy2

Go back to Sodium Binding Sites List in 8uy2
Sodium binding site 1 out of 1 in the Methylenetetrahydrofolate Reductase From Chaetomium Thermophilum Dsm 1495, Adomet-Bound, Inhibited (T) State


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Methylenetetrahydrofolate Reductase From Chaetomium Thermophilum Dsm 1495, Adomet-Bound, Inhibited (T) State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na707

b:81.3
occ:1.00
 O A:HOH830 2.4 65.8 1.0
O A:HOH868 2.5 43.6 1.0
OE1 A:GLU11 2.9 116.9 1.0
H A:ARG271 3.2 49.0 1.0
HB2 A:GLU11 3.4 77.4 1.0
HB3 A:PRO207 3.6 45.9 1.0
HB3 A:LEU7 3.6 44.4 1.0
H A:HIS272 3.8 46.4 1.0
HB2 A:PRO207 3.8 45.0 1.0
O A:HOH901 3.9 77.5 1.0
HB2 A:ARG271 3.9 50.6 1.0
HD22 A:LEU7 4.0 50.0 1.0
CD A:GLU11 4.0 121.2 1.0
HA A:ILE270 4.0 52.2 1.0
O A:LEU7 4.1 53.5 1.0
N A:ARG271 4.1 49.7 1.0
CB A:PRO207 4.1 45.4 1.0
O A:ILE208 4.2 53.1 1.0
HG22 A:ILE270 4.2 52.6 1.0
H A:ILE208 4.2 49.2 1.0
HB3 A:HIS272 4.3 44.3 1.0
CB A:GLU11 4.3 77.3 1.0
HA A:PRO207 4.4 47.3 1.0
N A:HIS272 4.5 46.5 1.0
HB2 A:ALA10 4.5 59.0 1.0
CB A:LEU7 4.5 43.2 1.0
HB2 A:HIS272 4.6 44.9 1.0
HA A:LEU7 4.6 45.8 1.0
CG A:GLU11 4.6 95.2 1.0
HA A:GLU11 4.6 66.2 1.0
C A:LEU7 4.7 47.0 1.0
H A:GLU11 4.7 58.0 1.0
HD13 A:LEU7 4.7 48.4 1.0
CA A:PRO207 4.7 45.8 1.0
CB A:ARG271 4.8 51.9 1.0
N A:ILE208 4.8 50.2 1.0
HG2 A:ARG271 4.8 52.4 1.0
CA A:ILE270 4.8 52.9 1.0
HG2 A:GLU11 4.8 95.9 1.0
CB A:HIS272 4.9 44.7 1.0
CD2 A:LEU7 4.9 51.5 1.0
CA A:LEU7 4.9 44.4 1.0
CA A:ARG271 4.9 48.1 1.0
CA A:GLU11 4.9 67.1 1.0
C A:ILE270 4.9 48.6 1.0
HB3 A:GLU11 5.0 78.3 1.0
N A:GLU11 5.0 56.5 1.0
OE2 A:GLU11 5.0 128.6 1.0

Reference:

J.Mendoza, K.Yamada, M.Koutmos. Structural Basis of S-Adenosylmethionine-Dependent Allosteric Transition From Active to Inactive States in Methylenetetrahydrofolate Reductase Nat Commun 2024.
ISSN: ESSN 2041-1723
DOI: 10.1038/S41467-024-49327-5
Page generated: Wed Oct 9 13:55:39 2024

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