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Potassium in PDB 2vlh: Quinonoid Intermediate of Citrobacter Freundii Tyrosine Phenol-Lyase Formed with Methionine

Enzymatic activity of Quinonoid Intermediate of Citrobacter Freundii Tyrosine Phenol-Lyase Formed with Methionine

All present enzymatic activity of Quinonoid Intermediate of Citrobacter Freundii Tyrosine Phenol-Lyase Formed with Methionine:
4.1.99.2;

Protein crystallography data

The structure of Quinonoid Intermediate of Citrobacter Freundii Tyrosine Phenol-Lyase Formed with Methionine, PDB code: 2vlh was solved by D.Milic, T.V.Demidkina, D.Matkovic-Calogovic, A.A.Antson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 97.59 / 1.95
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 132.886, 143.284, 59.665, 90.00, 90.00, 90.00
R / Rfree (%) 15.5 / 19.2

Potassium Binding Sites:

The binding sites of Potassium atom in the Quinonoid Intermediate of Citrobacter Freundii Tyrosine Phenol-Lyase Formed with Methionine (pdb code 2vlh). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Quinonoid Intermediate of Citrobacter Freundii Tyrosine Phenol-Lyase Formed with Methionine, PDB code: 2vlh:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 2vlh

Go back to Potassium Binding Sites List in 2vlh
Potassium binding site 1 out of 2 in the Quinonoid Intermediate of Citrobacter Freundii Tyrosine Phenol-Lyase Formed with Methionine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Quinonoid Intermediate of Citrobacter Freundii Tyrosine Phenol-Lyase Formed with Methionine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1458

b:19.8
occ:1.00
OE1 B:GLU69 2.7 29.6 1.0
O B:HOH2311 2.8 17.6 1.0
O A:GLY52 2.8 32.0 1.0
O A:HOH2083 2.9 18.8 1.0
O A:ASN262 2.9 32.2 1.0
O A:HOH2278 3.2 22.6 1.0
O B:GLU69 3.2 30.3 1.0
C A:GLY52 3.6 32.1 1.0
CB B:GLU69 3.8 25.7 1.0
CD B:GLU69 3.8 29.4 1.0
C A:ASN262 3.9 31.1 1.0
CA A:GLY52 3.9 30.1 1.0
C B:GLU69 3.9 28.0 1.0
CB A:ASN262 4.0 28.3 1.0
CA B:GLU69 4.0 27.9 1.0
CA A:ASN262 4.1 31.2 1.0
O B:HOH2102 4.2 19.0 1.0
CG B:GLU69 4.2 25.8 1.0
CA B:ALA295 4.3 30.0 1.0
N B:GLY296 4.4 29.8 1.0
N A:THR53 4.7 29.4 1.0
ND2 A:ASN262 4.8 28.6 1.0
CE A:LYS256 4.8 29.9 1.0
CG A:ASN262 4.8 32.0 1.0
OE2 B:GLU69 4.9 30.9 1.0
CB B:ALA295 4.9 28.5 1.0
O B:LEU294 4.9 29.6 1.0
C B:ALA295 4.9 31.6 1.0
O B:ALA70 5.0 30.3 1.0

Potassium binding site 2 out of 2 in 2vlh

Go back to Potassium Binding Sites List in 2vlh
Potassium binding site 2 out of 2 in the Quinonoid Intermediate of Citrobacter Freundii Tyrosine Phenol-Lyase Formed with Methionine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Quinonoid Intermediate of Citrobacter Freundii Tyrosine Phenol-Lyase Formed with Methionine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K1458

b:20.2
occ:1.00
O A:HOH2299 2.7 17.3 1.0
OE1 A:GLU69 2.8 31.1 1.0
O B:ASN262 2.8 30.1 1.0
O A:HOH2100 2.9 19.8 1.0
O B:GLY52 2.9 30.8 1.0
O B:HOH2289 3.1 18.5 1.0
O A:GLU69 3.4 30.1 1.0
C B:GLY52 3.7 31.9 1.0
C B:ASN262 3.8 30.6 1.0
CB A:GLU69 3.9 28.0 1.0
CA B:GLY52 3.9 31.7 1.0
CD A:GLU69 3.9 30.2 1.0
CB B:ASN262 4.0 29.7 1.0
CA B:ASN262 4.1 30.6 1.0
C A:GLU69 4.1 28.9 1.0
CA A:GLU69 4.2 27.4 1.0
CA A:ALA295 4.2 30.3 1.0
CG A:GLU69 4.4 28.2 1.0
O A:HOH2103 4.4 21.5 1.0
N A:GLY296 4.4 29.3 1.0
O A:LEU294 4.7 30.4 1.0
CE B:LYS256 4.7 28.8 1.0
CB A:ALA295 4.8 29.1 1.0
N B:THR53 4.8 32.4 1.0
C A:ALA295 4.9 30.3 1.0
O B:SER51 4.9 33.0 1.0
ND2 B:ASN262 4.9 27.8 1.0
CG B:ASN262 4.9 33.3 1.0

Reference:

D.Milic, T.V.Demidkina, N.G.Faleev, D.Matkovic-Calogovic, A.A.Antson. Insights Into the Catalytic Mechanism of Tyrosine Phenol-Lyase From X-Ray Structures of Quinonoid Intermediates. J.Biol.Chem. V. 283 29206 2008.
ISSN: ISSN 0021-9258
PubMed: 18715865
DOI: 10.1074/JBC.M802061200
Page generated: Sun Dec 13 23:12:39 2020

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