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Sodium in PDB 1knr: L-Aspartate Oxidase: R386L Mutant

Enzymatic activity of L-Aspartate Oxidase: R386L Mutant

All present enzymatic activity of L-Aspartate Oxidase: R386L Mutant:
1.4.3.16;

Protein crystallography data

The structure of L-Aspartate Oxidase: R386L Mutant, PDB code: 1knr was solved by R.T.Bossi, A.Mattevi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 2.50
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 73.278, 73.278, 313.933, 90.00, 90.00, 90.00
R / Rfree (%) 25 / 29.5

Other elements in 1knr:

The structure of L-Aspartate Oxidase: R386L Mutant also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the L-Aspartate Oxidase: R386L Mutant (pdb code 1knr). 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 L-Aspartate Oxidase: R386L Mutant, PDB code: 1knr:

Sodium binding site 1 out of 1 in 1knr

Go back to Sodium Binding Sites List in 1knr
Sodium binding site 1 out of 1 in the L-Aspartate Oxidase: R386L Mutant


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of L-Aspartate Oxidase: R386L Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na542

b:71.9
occ:1.00
O A:GLU375 2.2 73.9 1.0
O A:SER377 2.4 71.3 1.0
O A:GLY355 2.6 72.2 1.0
O A:THR353 2.8 69.5 1.0
C A:GLU375 3.1 72.7 1.0
C A:SER377 3.6 71.5 1.0
CA A:GLU375 3.6 71.8 1.0
C A:GLY355 3.8 71.0 1.0
C A:CYS354 3.8 71.3 1.0
O A:CYS354 3.8 69.9 1.0
N A:SER377 3.9 70.5 1.0
C A:THR353 4.0 71.2 1.0
O A:GLY374 4.1 73.7 1.0
OH A:TYR352 4.2 78.8 1.0
N A:GLY355 4.2 72.2 1.0
N A:VAL376 4.2 72.0 1.0
CA A:CYS354 4.3 72.4 1.0
CG A:GLU375 4.3 75.8 1.0
CA A:SER377 4.3 70.7 1.0
C A:VAL376 4.3 71.1 1.0
O A:HOH808 4.4 84.9 1.0
OG A:SER377 4.4 69.5 1.0
CB A:GLU375 4.5 72.4 1.0
CA A:GLY355 4.5 70.7 1.0
N A:TYR378 4.6 71.2 1.0
CZ A:TYR352 4.6 66.4 1.0
N A:CYS354 4.6 71.3 1.0
CE2 A:TYR352 4.6 70.2 1.0
N A:GLU375 4.7 71.7 1.0
OE1 A:GLU394 4.7 70.3 1.0
CA A:VAL376 4.8 70.4 1.0
N A:GLY356 4.8 69.7 1.0
C A:GLY374 4.8 72.8 1.0
CD2 A:HIS382 4.8 71.9 1.0
CA A:TYR378 4.8 72.0 1.0
CB A:THR353 4.8 71.0 1.0
O A:VAL376 4.9 72.3 1.0
CA A:GLY356 5.0 69.6 1.0

Reference:

R.T.Bossi, A.Negri, G.Tedeschi, A.Mattevi. Structure of Fad-Bound L-Aspartate Oxidase: Insight Into Substrate Specificity and Catalysis. Biochemistry V. 41 3018 2002.
ISSN: ISSN 0006-2960
PubMed: 11863440
DOI: 10.1021/BI015939R
Page generated: Tue Dec 15 05:28:37 2020

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