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Potassium in PDB 2yct: Tyrosine Phenol-Lyase From Citrobacter Freundii in Complex with Pyridine N-Oxide and the Quinonoid Intermediate Formed with L-Alanine

Enzymatic activity of Tyrosine Phenol-Lyase From Citrobacter Freundii in Complex with Pyridine N-Oxide and the Quinonoid Intermediate Formed with L-Alanine

All present enzymatic activity of Tyrosine Phenol-Lyase From Citrobacter Freundii in Complex with Pyridine N-Oxide and the Quinonoid Intermediate Formed with L-Alanine:
4.1.99.2;

Protein crystallography data

The structure of Tyrosine Phenol-Lyase From Citrobacter Freundii in Complex with Pyridine N-Oxide and the Quinonoid Intermediate Formed with L-Alanine, PDB code: 2yct was solved by D.Milic, T.V.Demidkina, N.G.Faleev, R.S.Phillips, 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) 20.00 / 2.25
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 133.993, 143.770, 60.081, 90.00, 90.00, 90.00
R / Rfree (%) 13.9 / 18.1

Potassium Binding Sites:

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

Potassium binding site 1 out of 2 in 2yct

Go back to Potassium Binding Sites List in 2yct
Potassium binding site 1 out of 2 in the Tyrosine Phenol-Lyase From Citrobacter Freundii in Complex with Pyridine N-Oxide and the Quinonoid Intermediate Formed with L-Alanine


Mono view


Stereo pair view

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

b:16.1
occ:1.00
 OE1 B:GLU69 2.8 14.7 1.0
O A:GLY52 2.8 16.6 1.0
O B:HOH2282 2.8 12.3 1.0
O A:HOH2069 2.9 14.1 1.0
O A:ASN262 2.9 18.2 1.0
O A:HOH2240 3.2 20.7 1.0
O B:GLU69 3.2 19.4 1.0
C A:GLY52 3.6 17.0 1.0
CB B:GLU69 3.8 14.5 1.0
CD B:GLU69 3.9 15.7 1.0
C A:ASN262 3.9 18.6 1.0
CB A:ASN262 3.9 15.2 1.0
CA A:GLY52 3.9 15.4 1.0
C B:GLU69 4.0 18.6 1.0
CA B:GLU69 4.0 16.5 1.0
CA A:ASN262 4.1 18.0 1.0
O B:HOH2093 4.2 14.5 1.0
CG B:GLU69 4.3 15.3 1.0
CA B:ALA295 4.4 16.5 1.0
N B:GLY296 4.5 17.7 1.0
N A:THR53 4.8 15.9 1.0
ND2 A:ASN262 4.8 15.5 1.0
CG A:ASN262 4.8 15.2 1.0
O B:ALA70 4.9 18.5 1.0
CE A:LYS256 4.9 18.4 1.0
CB B:ALA295 4.9 13.2 1.0
C B:ALA295 4.9 17.9 1.0
OE2 B:GLU69 4.9 17.1 1.0
O B:LEU294 5.0 18.3 1.0

Potassium binding site 2 out of 2 in 2yct

Go back to Potassium Binding Sites List in 2yct
Potassium binding site 2 out of 2 in the Tyrosine Phenol-Lyase From Citrobacter Freundii in Complex with Pyridine N-Oxide and the Quinonoid Intermediate Formed with L-Alanine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Tyrosine Phenol-Lyase From Citrobacter Freundii in Complex with Pyridine N-Oxide and the Quinonoid Intermediate Formed with L-Alanine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K1457

b:13.8
occ:1.00
 O A:HOH2259 2.7 6.3 1.0
OE1 A:GLU69 2.7 15.2 1.0
O B:GLY52 2.8 15.8 1.0
O B:ASN262 2.9 16.2 1.0
O A:HOH2088 3.0 13.1 1.0
O B:HOH2255 3.1 14.0 1.0
O A:GLU69 3.5 19.6 1.0
C B:GLY52 3.7 18.6 1.0
CB A:GLU69 3.7 12.8 1.0
CD A:GLU69 3.8 18.2 1.0
CB B:ASN262 3.8 14.1 1.0
C B:ASN262 3.9 17.1 1.0
CA B:GLY52 4.0 16.9 1.0
CA B:ASN262 4.1 15.7 1.0
CA A:GLU69 4.1 14.9 1.0
C A:GLU69 4.2 16.1 1.0
CG A:GLU69 4.2 13.2 1.0
CA A:ALA295 4.2 18.8 1.0
O A:HOH2091 4.4 16.2 1.0
N A:GLY296 4.5 16.4 1.0
O A:LEU294 4.7 20.3 1.0
ND2 B:ASN262 4.8 14.7 1.0
CG B:ASN262 4.8 17.7 1.0
CB A:ALA295 4.8 14.9 1.0
N B:THR53 4.8 19.3 1.0
OE2 A:GLU69 4.9 13.9 1.0
C A:ALA295 4.9 17.7 1.0
CE B:LYS256 4.9 16.5 1.0
O B:SER51 4.9 17.8 1.0

Reference:

D.Milic, T.V.Demidkina, N.G.Faleev, R.S.Phillips, D.Matkovic-Calogovic, A.A.Antson. Crystallographic Snapshots of Tyrosine Phenol-Lyase Show That Substrate Strain Plays A Role in C-C Bond Cleavage J.Am.Chem.Soc. V. 133 16468 2011.
ISSN: ISSN 0002-7863
PubMed: 21899319
DOI: 10.1021/JA203361G
Page generated: Sun Dec 13 23:13:54 2020

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