Sodium in PDB 1knp: E. Coli L-Aspartate Oxidase: Mutant R386L in Complex with Succinate

All present enzymatic activity of E. Coli L-Aspartate Oxidase: Mutant R386L in Complex with Succinate:
1.4.3.16;

The structure of E. Coli L-Aspartate Oxidase: Mutant R386L in Complex with Succinate, PDB code: 1knp 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 / 2.60
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	72.540, 72.540, 309.120, 90.00, 90.00, 90.00
R / Rfree (%)	23 / 28.1

The binding sites of Sodium atom in the E. Coli L-Aspartate Oxidase: Mutant R386L in Complex with Succinate (pdb code 1knp). 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 E. Coli L-Aspartate Oxidase: Mutant R386L in Complex with Succinate, PDB code: 1knp:

Sodium binding site 1 out of 1 in the E. Coli L-Aspartate Oxidase: Mutant R386L in Complex with Succinate


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of E. Coli L-Aspartate Oxidase: Mutant R386L in Complex with Succinate within 5.0Å range: probe atom residue distance (Å) B Occ A:Na541 b:32.7 occ:1.00 O A:HOH812 0.9 0.0 1.0 O A:GLU375 2.0 49.3 1.0 O A:GLY355 2.3 49.6 1.0 O A:SER377 2.3 45.1 1.0 O A:THR353 2.5 45.0 1.0 C A:GLU375 2.9 49.9 1.0 C A:SER377 3.4 49.4 1.0 C A:GLY355 3.4 52.4 1.0 N A:SER377 3.5 49.8 1.0 CA A:GLU375 3.6 51.0 1.0 C A:THR353 3.8 49.7 1.0 O A:CYS354 3.9 49.3 1.0 C A:CYS354 3.9 50.0 1.0 C A:VAL376 3.9 50.1 1.0 CA A:SER377 4.0 49.8 1.0 N A:VAL376 4.0 49.7 1.0 O A:GLY374 4.1 53.4 1.0 N A:GLY355 4.2 50.9 1.0 CG A:GLU375 4.2 56.6 1.0 CA A:VAL376 4.3 48.6 1.0 CA A:GLY355 4.3 51.5 1.0 CB A:THR353 4.3 49.9 1.0 N A:GLY356 4.4 53.4 1.0 CB A:GLU375 4.5 50.4 1.0 CA A:CYS354 4.5 49.9 1.0 N A:TYR378 4.5 49.9 1.0 CA A:GLY356 4.6 53.6 1.0 CG2 A:THR353 4.6 44.3 1.0 O A:VAL376 4.6 53.0 1.0 N A:CYS354 4.6 48.6 1.0 OG A:SER377 4.6 53.9 1.0 OH A:TYR352 4.7 50.6 1.0 N A:GLU375 4.7 51.2 1.0 CA A:THR353 4.7 48.8 1.0 C A:GLY374 4.8 52.8 1.0 CZ A:TYR352 4.9 47.2 1.0 CA A:TYR378 5.0 50.1 1.0 CB A:SER377 5.0 49.2 1.0

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