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

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

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

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

Sodium

(Na)

1 atom

The binding sites of Chlorine atom in the L-Aspartate Oxidase: R386L Mutant (pdb code 1knr). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the L-Aspartate Oxidase: R386L Mutant, PDB code: 1knr:

Chlorine binding site 1 out of 1 in the L-Aspartate Oxidase: R386L Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of L-Aspartate Oxidase: R386L Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl541 b:78.0 occ:1.00 OG1 A:THR259 3.0 90.1 1.0 N A:GLU260 3.5 87.2 1.0 NE2 A:HIS244 3.6 88.0 1.0 CA A:THR259 3.7 87.4 1.0 NH2 A:ARG290 3.8 85.2 1.0 CB A:THR259 3.9 87.6 1.0 CD2 A:LEU257 4.0 85.6 1.0 OE1 A:GLU121 4.0 92.3 1.0 C A:THR259 4.1 87.7 1.0 N5 A:FAD800 4.2 78.4 1.0 N A:GLY51 4.4 88.7 1.0 CE1 A:HIS244 4.5 83.7 1.0 O4 A:FAD800 4.6 80.2 1.0 CD2 A:HIS244 4.6 82.8 1.0 CB A:GLU260 4.6 86.4 1.0 CA A:GLU260 4.6 86.8 1.0 CA A:GLY51 4.7 88.3 1.0 C5X A:FAD800 4.7 77.5 1.0 OE2 A:GLU121 4.7 91.1 1.0 CG A:LEU257 4.7 89.2 1.0 C4X A:FAD800 4.7 80.1 1.0 CD A:GLU121 4.8 88.4 1.0 N A:THR259 4.9 86.8 1.0 CD1 A:LEU257 4.9 89.8 1.0 CB A:GLN50 4.9 88.4 1.0 C6 A:FAD800 4.9 74.2 1.0 C4 A:FAD800 4.9 80.5 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