Atomistry » Potassium » PDB 4qxg-4tog » 4r33
Atomistry »
  Potassium »
    PDB 4qxg-4tog »
      4r33 »

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

Protein crystallography data

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

Other elements in 4r33:

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

Potassium Binding Sites:

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 4r33

Go back to Potassium Binding Sites List in 4r33
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 4r33

Go back to Potassium Binding Sites List in 4r33
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

Reference:

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
Page generated: Sun Dec 13 23:48:39 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy