Atomistry » Sodium » PDB 5zxe-6ah7 » 6aa9
Atomistry »
  Sodium »
    PDB 5zxe-6ah7 »
      6aa9 »

Sodium in PDB 6aa9: T166A Mutant of D-Serine Deaminase From Salmonella Typhimurium

Enzymatic activity of T166A Mutant of D-Serine Deaminase From Salmonella Typhimurium

All present enzymatic activity of T166A Mutant of D-Serine Deaminase From Salmonella Typhimurium:
4.3.1.18;

Protein crystallography data

The structure of T166A Mutant of D-Serine Deaminase From Salmonella Typhimurium, PDB code: 6aa9 was solved by G.Deka, S.R.Bharath, H.S.Shavithri, M.R.N.Murthy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 53.20 / 2.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 108.310, 46.140, 99.280, 90.00, 100.80, 90.00
R / Rfree (%) 28.9 / 34.9

Sodium Binding Sites:

The binding sites of Sodium atom in the T166A Mutant of D-Serine Deaminase From Salmonella Typhimurium (pdb code 6aa9). 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 T166A Mutant of D-Serine Deaminase From Salmonella Typhimurium, PDB code: 6aa9:

Sodium binding site 1 out of 1 in 6aa9

Go back to Sodium Binding Sites List in 6aa9
Sodium binding site 1 out of 1 in the T166A Mutant of D-Serine Deaminase From Salmonella Typhimurium


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of T166A Mutant of D-Serine Deaminase From Salmonella Typhimurium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na501

b:18.1
occ:1.00
O A:SER307 2.8 20.0 1.0
O A:GLY277 2.9 14.7 1.0
OE2 A:GLU303 3.1 17.2 1.0
O A:LEU338 3.1 20.5 1.0
SG A:CYS309 3.1 20.3 1.0
O A:CYS276 3.2 14.3 1.0
O A:VAL340 3.5 20.9 1.0
C A:GLY277 3.7 14.6 1.0
CD A:GLU303 3.8 17.1 1.0
CA A:GLY277 3.9 14.6 1.0
C A:SER307 3.9 20.2 1.0
CG A:GLU303 4.0 17.0 1.0
C A:CYS276 4.0 14.3 1.0
CB A:SER307 4.1 20.3 1.0
CB A:VAL340 4.2 20.7 1.0
N A:CYS309 4.2 20.3 1.0
N A:VAL340 4.3 20.8 1.0
C A:LEU338 4.3 20.7 1.0
CB A:GLU303 4.3 16.8 1.0
N A:GLY277 4.4 14.5 1.0
C A:VAL340 4.4 21.1 1.0
CB A:CYS309 4.4 20.3 1.0
CA A:VAL340 4.5 20.8 1.0
CD A:PRO304 4.5 17.5 1.0
CA A:SER307 4.7 20.3 1.0
SG A:CYS276 4.8 14.2 1.0
CA A:LEU338 4.8 20.8 1.0
OE1 A:GLU303 4.8 17.2 1.0
N A:PRO308 4.9 20.2 1.0
CB A:LEU338 4.9 20.6 1.0
CA A:CYS309 4.9 20.2 1.0
N A:MET310 5.0 20.1 1.0
N A:VAL278 5.0 14.5 1.0
CA A:PRO308 5.0 20.2 1.0

Reference:

G.Deka, S.R.Bharath, H.S.Shavithri, M.R.N.Murthy. Structural Studies on the Decameric S. Typhimurium Arginine Decarboxylase (Adc): Pyridoxal 5'-Phosphate Binding Induces Conformational Changes Biochem. Biophys. Res. V. 490 1362 2017COMMUN..
ISSN: ESSN 1090-2104
PubMed: 28694189
DOI: 10.1016/J.BBRC.2017.07.032
Page generated: Tue Oct 8 01:46:45 2024

Last articles

W in 8QLN
W in 8RJA
V in 8WTN
Te in 8QLN
Re in 9GHX
Rb in 8Z5C
Ni in 9C0T
Ni in 9C0S
Ni in 9GP1
Ni in 9FYO
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy