Caesium in PDB 7tcs: M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine

All present enzymatic activity of M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine:
4.1.99.2;

The structure of M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine, PDB code: 7tcs 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)	45.27 / 1.37
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	63.55, 82.99, 96.58, 93.73, 105.71, 114.24
R / Rfree (%)	14.1 / 15.5

The structure of M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine also contains other interesting chemical elements:

Potassium

(K)

4 atoms

The binding sites of Caesium atom in the M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine (pdb code 7tcs). This binding sites where shown within 5.0 Angstroms radius around Caesium atom.
In total 3 binding sites of Caesium where determined in the M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine, PDB code: 7tcs:
Jump to Caesium binding site number: 1; 2; 3;

Caesium binding site 1 out of 3 in the M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine


Mono view


Stereo pair view

A full contact list of Caesium with other atoms in the Cs binding site number 1 of M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine within 5.0Å range: probe atom residue distance (Å) B Occ A:Cs505 b:196.5 occ:1.00 O C:HOH734 2.8 85.8 1.0 O C:HOH746 3.8 50.4 1.0 HB2 A:TYR3 4.1 30.2 1.0 O C:HOH966 4.1 32.5 0.6 OD2 C:ASP418 4.1 28.0 1.0 HE1 A:TYR324 4.2 31.7 1.0 HD2 A:TYR414 4.2 23.6 1.0 CD2 A:TYR414 4.3 19.6 1.0 O A:HOH976 4.3 56.9 1.0 HB2 C:ALA415 4.5 23.5 1.0 HB3 A:TYR414 4.5 22.0 1.0 HB3 A:TYR3 4.5 30.2 1.0 CG A:TYR414 4.6 17.6 1.0 CE1 A:TYR324 4.6 26.4 1.0 HB2 A:TYR414 4.7 22.0 1.0 CE2 A:TYR414 4.7 20.0 1.0 HD2 A:TYR3 4.7 27.9 1.0 O A:HOH770 4.7 43.0 1.0 CB A:TYR3 4.7 25.2 1.0 HA C:ALA415 4.7 20.9 1.0 CB A:TYR414 4.8 18.3 1.0 HE2 A:TYR414 4.9 24.1 1.0 O A:TYR3 4.9 25.0 1.0

Caesium binding site 2 out of 3 in the M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine


Mono view


Stereo pair view

A full contact list of Caesium with other atoms in the Cs binding site number 2 of M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine within 5.0Å range: probe atom residue distance (Å) B Occ C:Cs505 b:187.4 occ:1.00 HE1 C:TYR324 3.6 32.0 1.0 O A:HOH770 4.0 43.0 1.0 HB2 C:TYR3 4.0 30.6 1.0 CE1 C:TYR324 4.0 26.6 1.0 O C:HOH746 4.1 50.4 1.0 HD2 C:TYR3 4.3 31.0 1.0 HB3 C:TYR414 4.4 22.1 1.0 O A:HOH963 4.4 26.9 0.6 O C:HOH625 4.5 51.6 1.0 HB3 C:TYR3 4.5 30.6 1.0 CD2 C:TYR414 4.5 21.0 1.0 CZ C:TYR324 4.5 24.9 1.0 OH C:TYR324 4.5 26.9 1.0 HD2 C:TYR414 4.6 25.3 1.0 CG C:TYR414 4.6 18.8 1.0 CB C:TYR3 4.7 25.4 1.0 CD1 C:TYR324 4.7 26.2 1.0 HD1 C:TYR324 4.7 31.5 1.0 HB2 C:TYR414 4.7 22.1 1.0 OD2 A:ASP418 4.7 31.4 1.0 CB C:TYR414 4.8 18.4 1.0 CD2 C:TYR3 4.9 25.8 1.0 CE2 C:TYR414 5.0 22.1 1.0

Caesium binding site 3 out of 3 in the M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine


Mono view


Stereo pair view

A full contact list of Caesium with other atoms in the Cs binding site number 3 of M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine within 5.0Å range: probe atom residue distance (Å) B Occ D:Cs503 b:193.6 occ:1.00 O B:HOH852 2.7 70.8 1.0 O D:HOH969 2.8 84.0 1.0 O D:HOH883 2.8 80.3 1.0 HE1 D:TYR324 3.7 30.2 1.0 HB2 D:TYR3 3.8 32.1 1.0 HD2 D:TYR3 4.1 29.3 1.0 O B:HOH697 4.1 40.6 1.0 CE1 D:TYR324 4.2 25.1 1.0 O B:HOH801 4.2 58.8 1.0 O D:HOH734 4.4 62.1 1.0 O B:HOH898 4.4 31.8 1.0 O B:HOH883 4.5 65.1 1.0 HB3 D:TYR3 4.5 32.1 1.0 HB3 D:TYR414 4.5 20.4 1.0 CD2 D:TYR414 4.6 21.2 1.0 CB D:TYR3 4.6 26.7 1.0 HD2 D:TYR414 4.6 25.5 1.0 CG D:TYR414 4.7 17.8 1.0 OH D:TYR324 4.7 27.1 1.0 CZ D:TYR324 4.7 27.3 1.0 CD2 D:TYR3 4.8 24.4 1.0 HD1 D:TYR324 4.8 27.6 1.0 CD1 D:TYR324 4.8 23.0 1.0 HB2 D:TYR414 4.8 20.4 1.0 O D:HOH693 4.8 46.8 1.0 OD2 B:ASP418 4.9 32.7 1.0 CB D:TYR414 4.9 16.9 1.0 CE2 D:TYR414 4.9 21.2 1.0

R.S.Phillips, B.Jones, S.Nash. M379A Mutant Tyrosine Phenol-Lyase From Citrobacter Freundii Has Altered Conformational Dynamics. Chembiochem V. 23 00028 2022.
ISSN: ESSN 1439-7633
PubMed: 35577764
DOI: 10.1002/CBIC.202200028