Potassium in PDB 6mo3: Citrobacter Freundii Tyrosine Phenol-Lyase Complexed with 4- Hydroxypyridine and Aminoacrylate From L-Serine

Enzymatic activity of Citrobacter Freundii Tyrosine Phenol-Lyase Complexed with 4- Hydroxypyridine and Aminoacrylate From L-Serine

All present enzymatic activity of Citrobacter Freundii Tyrosine Phenol-Lyase Complexed with 4- Hydroxypyridine and Aminoacrylate From L-Serine:
4.1.99.2;

Protein crystallography data

The structure of Citrobacter Freundii Tyrosine Phenol-Lyase Complexed with 4- Hydroxypyridine and Aminoacrylate From L-Serine, PDB code: 6mo3 was solved by R.S.Phillips, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 55.12 / 1.79
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 59.680, 133.810, 143.780, 90.00, 90.00, 90.00
R / Rfree (%) 15.9 / 18.2

Potassium Binding Sites:

The binding sites of Potassium atom in the Citrobacter Freundii Tyrosine Phenol-Lyase Complexed with 4- Hydroxypyridine and Aminoacrylate From L-Serine (pdb code 6mo3). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Citrobacter Freundii Tyrosine Phenol-Lyase Complexed with 4- Hydroxypyridine and Aminoacrylate From L-Serine, PDB code: 6mo3:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 6mo3

Go back to Potassium Binding Sites List in 6mo3
Potassium binding site 1 out of 2 in the Citrobacter Freundii Tyrosine Phenol-Lyase Complexed with 4- Hydroxypyridine and Aminoacrylate From L-Serine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Citrobacter Freundii Tyrosine Phenol-Lyase Complexed with 4- Hydroxypyridine and Aminoacrylate From L-Serine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1604

b:30.0
occ:1.00
O B:HOH653 2.7 27.6 1.0
OE1 B:GLU69 2.7 26.9 1.0
O A:GLY52 2.9 25.8 1.0
O A:HOH1801 2.9 28.3 1.0
O A:ASN262 3.0 25.3 1.0
O A:HOH1875 3.1 35.6 1.0
O B:GLU69 3.2 30.2 1.0
C A:GLY52 3.7 26.4 1.0
CB B:GLU69 3.7 26.6 1.0
CD B:GLU69 3.9 26.1 1.0
CA B:GLU69 3.9 27.5 1.0
C B:GLU69 3.9 30.1 1.0
C A:ASN262 4.0 25.9 1.0
CB A:ASN262 4.0 21.8 1.0
CA A:GLY52 4.0 28.4 1.0
O B:HOH690 4.1 33.9 1.0
CA A:ASN262 4.2 24.0 1.0
CG B:GLU69 4.3 25.4 1.0
CA B:ALA295 4.3 28.3 1.0
N B:GLY296 4.4 26.8 1.0
ND2 A:ASN262 4.8 24.1 1.0
N A:THR53 4.8 24.4 1.0
CB B:ALA295 4.8 24.6 1.0
CE A:LYS256 4.8 29.7 1.0
CG A:ASN262 4.9 24.2 1.0
O B:LEU294 4.9 28.6 1.0
OE2 B:GLU69 4.9 25.0 1.0
C B:ALA295 4.9 28.7 1.0

Potassium binding site 2 out of 2 in 6mo3

Go back to Potassium Binding Sites List in 6mo3
Potassium binding site 2 out of 2 in the Citrobacter Freundii Tyrosine Phenol-Lyase Complexed with 4- Hydroxypyridine and Aminoacrylate From L-Serine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Citrobacter Freundii Tyrosine Phenol-Lyase Complexed with 4- Hydroxypyridine and Aminoacrylate From L-Serine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1605

b:31.4
occ:1.00
O A:HOH1778 2.7 27.4 1.0
OE1 A:GLU69 2.8 25.9 1.0
O A:HOH1807 2.8 28.0 1.0
O B:GLY52 2.9 25.9 1.0
O B:ASN262 2.9 26.1 1.0
O B:HOH765 3.0 31.6 1.0
O A:GLU69 3.4 29.0 1.0
C B:GLY52 3.7 28.6 1.0
CB A:GLU69 3.8 23.8 1.0
CD A:GLU69 3.9 28.1 1.0
C B:ASN262 3.9 26.0 1.0
CB B:ASN262 4.0 22.4 1.0
CA B:GLY52 4.0 26.4 1.0
CA A:GLU69 4.0 24.1 1.0
C A:GLU69 4.1 26.1 1.0
CA B:ASN262 4.2 22.8 1.0
O A:HOH1848 4.3 29.5 1.0
CA A:ALA295 4.3 26.8 1.0
CG A:GLU69 4.3 23.8 1.0
N A:GLY296 4.4 27.1 1.0
N B:THR53 4.8 27.7 1.0
O A:LEU294 4.8 27.9 1.0
CE B:LYS256 4.8 29.5 1.0
CB A:ALA295 4.8 24.3 1.0
ND2 B:ASN262 4.8 22.4 1.0
C A:ALA295 4.9 27.3 1.0
CG B:ASN262 4.9 25.9 1.0
O B:SER51 4.9 28.7 1.0
OE2 A:GLU69 5.0 25.7 1.0

Reference:

R.S.Phillips, R.S.Phillips. N/A N/A.
Page generated: Mon Dec 14 00:54:20 2020

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