Potassium in PDB 4r33: X-Ray Structure of the Tryptophan Lyase Nosl with Tryptophan and S- Adenosyl-L-Homocysteine Bound

The structure of X-Ray Structure of the Tryptophan Lyase Nosl with Tryptophan and S- Adenosyl-L-Homocysteine Bound, PDB code: 4r33 was solved by Y.Nicolet, L.Zeppieri, P.Amara, J.-C.Fontecilla-Camps, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.23 / 1.78
Space group	P 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	94.720, 47.230, 114.360, 90.00, 108.71, 90.00
R / Rfree (%)	15.9 / 18.1

The structure of X-Ray Structure of the Tryptophan Lyase Nosl with Tryptophan and S- Adenosyl-L-Homocysteine Bound also contains other interesting chemical elements:

Iron	(Fe)	8 atoms
Chlorine	(Cl)	2 atoms
Sodium	(Na)	1 atom

The binding sites of Potassium atom in the X-Ray Structure of the Tryptophan Lyase Nosl with Tryptophan and S- Adenosyl-L-Homocysteine Bound (pdb code 4r33). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the X-Ray Structure of the Tryptophan Lyase Nosl with Tryptophan and S- Adenosyl-L-Homocysteine Bound, PDB code: 4r33:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the X-Ray Structure of the Tryptophan Lyase Nosl with Tryptophan and S- Adenosyl-L-Homocysteine Bound


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of X-Ray Structure of the Tryptophan Lyase Nosl with Tryptophan and S- Adenosyl-L-Homocysteine Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:K505 b:28.1 occ:1.00 O A:PHE389 2.7 22.3 1.0 O A:VAL386 2.7 21.9 1.0 OE2 A:GLU380 2.7 21.8 1.0 O A:HOH634 2.9 31.9 1.0 O A:HOH628 3.2 33.1 1.0 C A:VAL386 3.7 22.2 1.0 CD A:GLU380 3.8 24.1 1.0 C A:PHE389 3.8 21.3 1.0 O A:HOH702 3.9 41.1 1.0 OE1 A:GLU380 4.1 25.8 1.0 N A:VAL386 4.1 21.3 1.0 O A:HOH765 4.1 47.2 1.0 CB A:PHE389 4.3 21.1 1.0 CA A:PHE389 4.4 19.9 1.0 N A:PHE389 4.4 23.6 1.0 CA A:VAL386 4.5 20.1 1.0 N A:ASP387 4.5 22.1 1.0 CD2 A:PHE389 4.6 19.7 1.0 CA A:ASP387 4.6 23.9 1.0 CG A:PHE389 4.9 20.6 1.0 N A:VAL390 4.9 21.1 1.0

Potassium binding site 2 out of 2 in the X-Ray Structure of the Tryptophan Lyase Nosl with Tryptophan and S- Adenosyl-L-Homocysteine Bound


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of X-Ray Structure of the Tryptophan Lyase Nosl with Tryptophan and S- Adenosyl-L-Homocysteine Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:K508 b:25.5 occ:0.83 OE2 B:GLU380 2.7 24.1 1.0 O B:VAL386 2.7 19.5 1.0 O B:PHE389 2.7 19.7 1.0 O B:HOH655 2.9 29.1 1.0 O B:HOH670 3.5 27.5 1.0 C B:VAL386 3.7 19.7 1.0 O B:HOH777 3.7 31.6 1.0 CD B:GLU380 3.7 23.8 1.0 C B:PHE389 3.9 19.5 1.0 OE1 B:GLU380 4.0 24.8 1.0 N B:VAL386 4.1 19.0 1.0 O B:HOH795 4.3 42.4 1.0 CA B:VAL386 4.4 18.8 1.0 N B:PHE389 4.5 18.3 1.0 CB B:PHE389 4.5 18.6 1.0 O B:HOH921 4.5 43.8 1.0 CA B:PHE389 4.5 18.5 1.0 N B:ASP387 4.5 20.6 1.0 O B:HOH761 4.6 45.3 1.0 CD2 B:PHE389 4.7 19.1 1.0 O B:HOH988 4.7 47.8 1.0 CA B:ASP387 4.7 20.0 1.0 N B:VAL390 5.0 17.4 1.0

Y.Nicolet, L.Zeppieri, P.Amara, J.C.Fontecilla-Camps. Crystal Structure of Tryptophan Lyase (Nosl): Evidence For Radical Formation at the Amino Group of Tryptophan. Angew.Chem.Int.Ed.Engl. V. 53 11840 2014.
ISSN: ISSN 1433-7851
PubMed: 25196319
DOI: 10.1002/ANIE.201407320