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Sodium in PDB 1y9d: Pyruvate Oxidase Variant V265A From Lactobacillus Plantarum

Enzymatic activity of Pyruvate Oxidase Variant V265A From Lactobacillus Plantarum

All present enzymatic activity of Pyruvate Oxidase Variant V265A From Lactobacillus Plantarum:
1.2.3.3;

Protein crystallography data

The structure of Pyruvate Oxidase Variant V265A From Lactobacillus Plantarum, PDB code: 1y9d was solved by G.Wille, M.Ritter, M.S.Weiss, S.Konig, W.Mantele, G.Hubner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.30 / 2.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 94.660, 155.780, 100.750, 90.00, 92.92, 90.00
R / Rfree (%) 17.8 / 23.8

Other elements in 1y9d:

The structure of Pyruvate Oxidase Variant V265A From Lactobacillus Plantarum also contains other interesting chemical elements:

Magnesium (Mg) 4 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Pyruvate Oxidase Variant V265A From Lactobacillus Plantarum (pdb code 1y9d). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Pyruvate Oxidase Variant V265A From Lactobacillus Plantarum, PDB code: 1y9d:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 1y9d

Go back to Sodium Binding Sites List in 1y9d
Sodium binding site 1 out of 2 in the Pyruvate Oxidase Variant V265A From Lactobacillus Plantarum


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Pyruvate Oxidase Variant V265A From Lactobacillus Plantarum within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na2605

b:48.9
occ:1.00
O A:HOH2858 2.7 36.0 1.0
O C:HOH2859 2.7 41.3 1.0
O A:MET452 2.8 33.8 1.0
OE1 A:GLN455 2.9 35.5 1.0
O C:MET452 2.9 34.8 1.0
OE1 C:GLN455 3.0 36.0 1.0
CD A:GLN455 3.7 36.9 1.0
CD C:GLN455 3.8 36.0 1.0
C A:MET452 3.9 34.4 1.0
CD2 C:HIS58 3.9 26.0 1.0
CD2 A:HIS58 3.9 25.8 1.0
C C:MET452 3.9 33.8 1.0
NE2 A:GLN455 4.1 36.4 1.0
NE2 C:GLN455 4.1 35.2 1.0
NE2 A:HIS58 4.6 26.4 1.0
NE2 C:HIS58 4.6 28.6 1.0
CA A:MET452 4.7 34.9 1.0
CG C:HIS58 4.7 28.6 1.0
O C:SER451 4.7 34.4 1.0
CG A:HIS58 4.7 28.2 1.0
CA C:MET452 4.7 33.2 1.0
CA A:THR453 4.7 33.9 1.0
O A:SER451 4.7 36.7 1.0
N A:THR453 4.7 34.1 1.0
N C:THR453 4.8 33.7 1.0
OE2 A:GLU60 4.8 42.4 1.0
CA C:THR453 4.9 33.7 1.0
CG A:GLN455 4.9 34.3 1.0
OE2 C:GLU60 4.9 39.6 1.0

Sodium binding site 2 out of 2 in 1y9d

Go back to Sodium Binding Sites List in 1y9d
Sodium binding site 2 out of 2 in the Pyruvate Oxidase Variant V265A From Lactobacillus Plantarum


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Pyruvate Oxidase Variant V265A From Lactobacillus Plantarum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na2705

b:42.9
occ:1.00
OE1 D:GLN455 2.7 33.2 1.0
OE1 B:GLN455 2.7 31.3 1.0
O D:HOH2971 2.8 38.8 1.0
O B:MET452 2.9 33.0 1.0
O B:HOH2971 2.9 37.3 1.0
O D:MET452 2.9 31.8 1.0
CD D:GLN455 3.6 32.0 1.0
CD B:GLN455 3.7 29.7 1.0
C B:MET452 3.9 32.0 1.0
C D:MET452 3.9 30.6 1.0
CD2 D:HIS58 4.0 21.6 1.0
CD2 B:HIS58 4.1 20.6 1.0
NE2 D:GLN455 4.1 29.0 1.0
NE2 B:GLN455 4.2 28.8 1.0
O D:SER451 4.6 31.9 1.0
O B:SER451 4.6 32.9 1.0
CA B:MET452 4.6 32.8 1.0
NE2 D:HIS58 4.7 25.8 1.0
CA D:MET452 4.7 30.8 1.0
N B:THR453 4.7 31.2 1.0
N D:THR453 4.7 29.1 1.0
CA B:THR453 4.7 29.2 1.0
CA D:THR453 4.7 29.5 1.0
CG D:HIS58 4.8 24.7 1.0
CG B:HIS58 4.8 21.6 1.0
NE2 B:HIS58 4.8 22.5 1.0
CG D:GLN455 4.8 30.4 1.0
OE2 D:GLU60 4.8 31.2 1.0
CG B:GLN455 4.8 31.2 1.0
OE2 B:GLU60 4.9 31.6 1.0

Reference:

G.Wille, M.Ritter, M.S.Weiss, S.Konig, W.Mantele, G.Hubner. The Role of Val-265 For Flavin Adenine Dinulceotide (Fad) Binding in Pyruvate Oxidase: Ftir, Kinetic and Crystallographic Studies on the Enzyme Variant V265A Biochemistry V. 44 5086 2005.
ISSN: ISSN 0006-2960
PubMed: 15794646
DOI: 10.1021/BI047337O
Page generated: Tue Dec 15 05:42:10 2020

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