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Potassium in PDB 2ycp: F448H Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii in Complex with Quinonoid Intermediate Formed with 3-Fluoro-L-Tyrosine

Enzymatic activity of F448H Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii in Complex with Quinonoid Intermediate Formed with 3-Fluoro-L-Tyrosine

All present enzymatic activity of F448H Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii in Complex with Quinonoid Intermediate Formed with 3-Fluoro-L-Tyrosine:
4.1.99.2;

Protein crystallography data

The structure of F448H Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii in Complex with Quinonoid Intermediate Formed with 3-Fluoro-L-Tyrosine, PDB code: 2ycp 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) 30.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 136.423, 143.757, 118.543, 90.00, 90.00, 90.00
R / Rfree (%) 14.1 / 17.5

Other elements in 2ycp:

The structure of F448H Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii in Complex with Quinonoid Intermediate Formed with 3-Fluoro-L-Tyrosine also contains other interesting chemical elements:

Fluorine (F) 4 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the F448H Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii in Complex with Quinonoid Intermediate Formed with 3-Fluoro-L-Tyrosine (pdb code 2ycp). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the F448H Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii in Complex with Quinonoid Intermediate Formed with 3-Fluoro-L-Tyrosine, PDB code: 2ycp:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 2ycp

Go back to Potassium Binding Sites List in 2ycp
Potassium binding site 1 out of 4 in the F448H Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii in Complex with Quinonoid Intermediate Formed with 3-Fluoro-L-Tyrosine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of F448H Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii in Complex with Quinonoid Intermediate Formed with 3-Fluoro-L-Tyrosine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1462

b:15.8
occ:1.00
 O B:HOH2321 2.7 14.6 1.0
OE1 B:GLU69 2.8 13.2 1.0
O A:HOH2094 2.8 13.5 1.0
O A:GLY52 2.8 15.1 1.0
O A:ASN262 2.9 13.9 1.0
O B:GLU69 3.2 19.0 1.0
O A:HOH2308 3.2 15.3 1.0
C A:GLY52 3.6 15.2 1.0
O B:HOH2115 3.8 17.6 1.0
CB B:GLU69 3.9 15.0 1.0
CD B:GLU69 3.9 15.6 1.0
C A:ASN262 3.9 14.3 1.0
C B:GLU69 3.9 17.4 1.0
CA A:GLY52 3.9 14.6 1.0
CB A:ASN262 4.0 13.8 1.0
CA B:GLU69 4.0 15.2 1.0
CA A:ASN262 4.1 14.6 1.0
CA B:ALA295 4.4 13.7 1.0
CG B:GLU69 4.4 13.0 1.0
N B:GLY296 4.5 14.5 1.0
N A:THR53 4.7 13.9 1.0
CE A:LYS256 4.7 13.8 1.0
ND2 A:ASN262 4.9 13.7 1.0
CB B:ALA295 4.9 13.7 1.0
O B:ALA70 4.9 16.1 1.0
CG A:ASN262 4.9 17.6 1.0
C B:ALA295 5.0 15.5 1.0
OE2 B:GLU69 5.0 17.1 1.0
O A:SER51 5.0 14.4 1.0

Potassium binding site 2 out of 4 in 2ycp

Go back to Potassium Binding Sites List in 2ycp
Potassium binding site 2 out of 4 in the F448H Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii in Complex with Quinonoid Intermediate Formed with 3-Fluoro-L-Tyrosine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of F448H Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii in Complex with Quinonoid Intermediate Formed with 3-Fluoro-L-Tyrosine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1463

b:16.3
occ:1.00
 O A:HOH2332 2.7 11.8 1.0
OE1 A:GLU69 2.7 15.6 1.0
O B:HOH2095 2.8 9.0 1.0
O B:GLY52 2.9 14.2 1.0
O B:ASN262 2.9 14.5 1.0
O A:GLU69 3.2 21.4 1.0
O B:HOH2295 3.3 14.6 1.0
C B:GLY52 3.6 14.3 1.0
CB A:GLU69 3.8 19.4 1.0
CD A:GLU69 3.8 17.0 1.0
O A:HOH2113 3.9 15.9 1.0
C B:ASN262 3.9 13.9 1.0
C A:GLU69 3.9 19.5 1.0
CA B:GLY52 3.9 14.3 1.0
CA A:GLU69 4.0 18.1 1.0
CB B:ASN262 4.0 11.2 1.0
CA B:ASN262 4.2 13.4 1.0
CG A:GLU69 4.3 15.3 1.0
CA A:ALA295 4.4 15.0 1.0
N A:GLY296 4.4 16.1 1.0
N B:THR53 4.7 14.2 1.0
O A:ALA70 4.7 19.2 1.0
ND2 B:ASN262 4.8 14.0 1.0
CE B:LYS256 4.8 13.9 1.0
CG B:ASN262 4.9 18.5 1.0
C A:ALA295 4.9 15.6 1.0
CB A:ALA295 4.9 12.6 1.0
OE2 A:GLU69 4.9 18.8 1.0
O A:LEU294 5.0 16.6 1.0
O B:SER51 5.0 16.1 1.0

Potassium binding site 3 out of 4 in 2ycp

Go back to Potassium Binding Sites List in 2ycp
Potassium binding site 3 out of 4 in the F448H Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii in Complex with Quinonoid Intermediate Formed with 3-Fluoro-L-Tyrosine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of F448H Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii in Complex with Quinonoid Intermediate Formed with 3-Fluoro-L-Tyrosine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K1463

b:17.1
occ:1.00
 OE1 D:GLU69 2.7 13.1 1.0
O D:HOH2305 2.8 14.5 1.0
O C:GLY52 2.8 15.6 1.0
O C:ASN262 2.8 12.4 1.0
O D:HOH2098 2.8 13.2 1.0
O D:GLU69 3.2 19.8 1.0
O C:HOH2299 3.3 17.5 1.0
C C:GLY52 3.6 16.6 1.0
CB D:GLU69 3.8 15.6 1.0
CD D:GLU69 3.8 15.4 1.0
C C:ASN262 3.8 13.7 1.0
C D:GLU69 3.9 19.1 1.0
O D:HOH2100 3.9 20.6 1.0
CA C:GLY52 3.9 15.7 1.0
CB C:ASN262 3.9 16.2 1.0
CA D:GLU69 3.9 16.9 1.0
CA C:ASN262 4.1 15.0 1.0
CG D:GLU69 4.3 14.0 1.0
CA D:ALA295 4.3 15.6 1.0
N D:GLY296 4.4 16.1 1.0
N C:THR53 4.7 16.3 1.0
CB D:ALA295 4.8 14.2 1.0
CE C:LYS256 4.8 12.4 1.0
O D:ALA70 4.8 17.4 1.0
ND2 C:ASN262 4.8 14.5 1.0
CG C:ASN262 4.9 16.2 1.0
OE2 D:GLU69 4.9 17.6 1.0
C D:ALA295 4.9 15.5 1.0

Potassium binding site 4 out of 4 in 2ycp

Go back to Potassium Binding Sites List in 2ycp
Potassium binding site 4 out of 4 in the F448H Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii in Complex with Quinonoid Intermediate Formed with 3-Fluoro-L-Tyrosine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of F448H Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii in Complex with Quinonoid Intermediate Formed with 3-Fluoro-L-Tyrosine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K1464

b:16.6
occ:1.00
 O C:HOH2325 2.6 12.7 1.0
OE1 C:GLU69 2.8 14.8 1.0
O D:HOH2079 2.9 10.2 1.0
O D:GLY52 2.9 15.3 1.0
O D:ASN262 3.0 15.1 1.0
O D:HOH2281 3.3 13.5 1.0
O C:GLU69 3.3 19.3 1.0
C D:GLY52 3.7 15.0 1.0
O C:HOH2105 3.7 21.3 1.0
CB C:GLU69 3.8 14.2 1.0
CD C:GLU69 3.9 16.1 1.0
C C:GLU69 3.9 18.3 1.0
CA C:GLU69 3.9 14.3 1.0
C D:ASN262 3.9 14.8 1.0
CA D:GLY52 4.0 14.4 1.0
CB D:ASN262 4.1 11.7 1.0
CA D:ASN262 4.2 13.1 1.0
CA C:ALA295 4.3 14.3 1.0
CG C:GLU69 4.3 11.1 1.0
N C:GLY296 4.4 14.2 1.0
O C:ALA70 4.8 15.9 1.0
CB C:ALA295 4.8 14.3 1.0
N D:THR53 4.9 14.1 1.0
CE D:LYS256 4.9 14.4 1.0
O C:LEU294 4.9 13.5 1.0
C C:ALA295 4.9 14.9 1.0
ND2 D:ASN262 4.9 12.1 1.0
OE2 C:GLU69 5.0 15.0 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: Mon Aug 12 07:42:45 2024

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