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Potassium in PDB 6mqq: Citrobacter Freundii F448A Mutant Tyrosine Phenol-Lyase Complexed with 4-Hydroxypyridine and Aminoacrylate From S-Ethyl-L-Cysteine

Enzymatic activity of Citrobacter Freundii F448A Mutant Tyrosine Phenol-Lyase Complexed with 4-Hydroxypyridine and Aminoacrylate From S-Ethyl-L-Cysteine

All present enzymatic activity of Citrobacter Freundii F448A Mutant Tyrosine Phenol-Lyase Complexed with 4-Hydroxypyridine and Aminoacrylate From S-Ethyl-L-Cysteine:
4.1.99.2;

Protein crystallography data

The structure of Citrobacter Freundii F448A Mutant Tyrosine Phenol-Lyase Complexed with 4-Hydroxypyridine and Aminoacrylate From S-Ethyl-L-Cysteine, PDB code: 6mqq 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) 45.96 / 2.05
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 59.560, 133.850, 144.520, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 19.7

Potassium Binding Sites:

The binding sites of Potassium atom in the Citrobacter Freundii F448A Mutant Tyrosine Phenol-Lyase Complexed with 4-Hydroxypyridine and Aminoacrylate From S-Ethyl-L-Cysteine (pdb code 6mqq). 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 F448A Mutant Tyrosine Phenol-Lyase Complexed with 4-Hydroxypyridine and Aminoacrylate From S-Ethyl-L-Cysteine, PDB code: 6mqq:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 6mqq

Go back to Potassium Binding Sites List in 6mqq
Potassium binding site 1 out of 2 in the Citrobacter Freundii F448A Mutant Tyrosine Phenol-Lyase Complexed with 4-Hydroxypyridine and Aminoacrylate From S-Ethyl-L-Cysteine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Citrobacter Freundii F448A Mutant Tyrosine Phenol-Lyase Complexed with 4-Hydroxypyridine and Aminoacrylate From S-Ethyl-L-Cysteine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K602

b:53.8
occ:1.00
 O B:GLY52 2.7 47.6 1.0
OE1 A:GLU69 2.7 46.6 1.0
O A:HOH761 2.8 47.4 1.0
O A:HOH750 2.9 54.0 1.0
O B:HOH1775 3.0 58.5 1.0
O B:ASN262 3.0 46.6 1.0
O A:GLU69 3.1 49.7 1.0
C B:GLY52 3.6 48.0 1.0
CB A:GLU69 3.7 45.4 1.0
CD A:GLU69 3.8 51.8 1.0
CA A:GLU69 3.9 43.2 1.0
C A:GLU69 3.9 47.7 1.0
CA B:GLY52 3.9 50.7 1.0
CB B:ASN262 3.9 41.8 1.0
C B:ASN262 4.0 49.3 1.0
CA B:ASN262 4.2 49.0 1.0
CG A:GLU69 4.2 48.9 1.0
O A:HOH731 4.2 46.8 1.0
CA A:ALA295 4.4 48.0 1.0
N A:GLY296 4.5 46.6 1.0
N B:THR53 4.7 47.3 1.0
ND2 B:ASN262 4.8 43.6 1.0
CE B:LYS256 4.8 50.8 1.0
CB A:ALA295 4.8 46.7 1.0
CG B:ASN262 4.8 44.2 1.0
O A:LEU294 4.9 46.4 1.0
OE2 A:GLU69 4.9 45.7 1.0
C A:ALA295 5.0 43.4 1.0

Potassium binding site 2 out of 2 in 6mqq

Go back to Potassium Binding Sites List in 6mqq
Potassium binding site 2 out of 2 in the Citrobacter Freundii F448A Mutant Tyrosine Phenol-Lyase Complexed with 4-Hydroxypyridine and Aminoacrylate From S-Ethyl-L-Cysteine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Citrobacter Freundii F448A Mutant Tyrosine Phenol-Lyase Complexed with 4-Hydroxypyridine and Aminoacrylate From S-Ethyl-L-Cysteine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K604

b:50.6
occ:1.00
 O B:HOH1729 2.8 45.0 1.0
O A:GLY52 2.8 47.9 1.0
OE1 B:GLU69 2.8 43.4 1.0
O A:HOH756 2.9 46.9 1.0
O A:HOH774 2.9 52.4 1.0
O A:ASN262 3.0 43.2 1.0
O B:GLU69 3.1 49.9 1.0
C A:GLY52 3.6 46.4 1.0
CB B:GLU69 3.8 44.7 1.0
CD B:GLU69 3.9 47.7 1.0
CA A:GLY52 3.9 48.7 1.0
C B:GLU69 3.9 50.0 1.0
CA B:GLU69 3.9 46.6 1.0
CB A:ASN262 4.0 46.0 1.0
C A:ASN262 4.0 46.4 1.0
O B:HOH1743 4.1 46.9 1.0
CA A:ASN262 4.2 46.8 1.0
CG B:GLU69 4.3 44.0 1.0
CA B:ALA295 4.4 46.2 1.0
N B:GLY296 4.5 46.7 1.0
N A:THR53 4.7 43.9 1.0
CE A:LYS256 4.7 46.6 1.0
ND2 A:ASN262 4.9 41.2 1.0
O B:LEU294 4.9 54.8 1.0
CG A:ASN262 4.9 43.4 1.0
CB B:ALA295 4.9 42.2 1.0
O B:ALA70 4.9 49.0 1.0
OE2 B:GLU69 5.0 41.3 1.0
C B:ALA295 5.0 46.8 1.0

Reference:

R.S.Phillips, R.S.Phillips. N/A N/A.
Page generated: Mon Dec 14 00:57:33 2020

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