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Sodium in PDB 6vmw: Crystal Structure of the F316A Mutant of Goxa Soaked with Glycine

Protein crystallography data

The structure of Crystal Structure of the F316A Mutant of Goxa Soaked with Glycine, PDB code: 6vmw was solved by E.T.Yukl, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.94 / 1.99
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 109.607, 91.883, 178.786, 90.00, 91.37, 90.00
R / Rfree (%) 17.2 / 22.3

Other elements in 6vmw:

The structure of Crystal Structure of the F316A Mutant of Goxa Soaked with Glycine also contains other interesting chemical elements:

Magnesium (Mg) 4 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the F316A Mutant of Goxa Soaked with Glycine (pdb code 6vmw). 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 the F316A Mutant of Goxa Soaked with Glycine, PDB code: 6vmw:

Sodium binding site 1 out of 1 in 6vmw

Go back to Sodium Binding Sites List in 6vmw
Sodium binding site 1 out of 1 in the Crystal Structure of the F316A Mutant of Goxa Soaked with Glycine


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 the F316A Mutant of Goxa Soaked with Glycine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na902

b:46.6
occ:1.00
OG B:SER440 2.1 36.5 1.0
O B:HOH1367 2.2 30.7 1.0
O B:HOH1470 2.4 41.1 1.0
O B:HOH1396 2.5 25.5 1.0
OG B:SER438 2.7 35.3 1.0
O B:HOH1495 2.9 42.7 1.0
CB B:SER440 3.4 34.1 1.0
CB B:SER438 3.6 30.8 1.0
N B:SER440 4.1 36.4 1.0
OD2 B:ASP436 4.2 38.2 1.0
CA B:SER440 4.3 32.9 1.0
OD1 B:ASP436 4.7 32.6 1.0
CA B:SER438 4.9 30.0 1.0
C B:SER438 4.9 32.5 1.0
CG B:ASP436 4.9 30.2 1.0
C B:SER440 5.0 29.5 1.0
N B:ALA439 5.0 30.1 1.0

Reference:

K.J.Mamounis, E.T.Yukl, V.L.Davidson. Roles of Active Site Residues in Catalysis, Substrate Binding, Cooperativity and the Reaction Mechanism of the Quinoprotein Glycine Oxidase J.Biol.Chem. 2020.
ISSN: ESSN 1083-351X
Page generated: Tue Oct 8 14:24:34 2024

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