Chlorine in PDB 7tdl: M379A Mutant Tyrosine Phenol-Lyase Complexed with 3-Bromo-Dl- Phenylalanine

All present enzymatic activity of M379A Mutant Tyrosine Phenol-Lyase Complexed with 3-Bromo-Dl- Phenylalanine:
4.1.99.2;

The structure of M379A Mutant Tyrosine Phenol-Lyase Complexed with 3-Bromo-Dl- Phenylalanine, PDB code: 7tdl 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)	58.41 / 1.60
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	61.25, 82.87, 94.33, 113.16, 96.54, 102.21
R / Rfree (%)	17.7 / 22.1

The structure of M379A Mutant Tyrosine Phenol-Lyase Complexed with 3-Bromo-Dl- Phenylalanine also contains other interesting chemical elements:

Bromine	(Br)	4 atoms
Potassium	(K)	4 atoms

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

Chlorine binding site 1 out of 3 in the M379A Mutant Tyrosine Phenol-Lyase Complexed with 3-Bromo-Dl- Phenylalanine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of M379A Mutant Tyrosine Phenol-Lyase Complexed with 3-Bromo-Dl- Phenylalanine within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl505 b:41.3 occ:1.00 HG22 B:VAL284 2.9 49.5 1.0 HA B:VAL284 3.2 45.3 1.0 HG22 A:THR125 3.2 40.5 1.0 HG22 A:THR124 3.2 53.3 1.0 HA A:THR125 3.2 38.5 1.0 HG12 B:VAL283 3.4 56.7 1.0 HB3 A:TYR128 3.6 46.6 1.0 HB2 A:TYR128 3.6 46.6 1.0 CG2 B:VAL284 3.8 41.2 1.0 HD21 A:LEU446 3.8 95.3 1.0 CB A:TYR128 3.9 38.9 1.0 CG A:TYR128 3.9 41.4 1.0 HG23 A:THR124 3.9 53.3 1.0 HG23 B:VAL284 3.9 49.5 1.0 CG2 A:THR124 4.0 44.4 1.0 CA B:VAL284 4.1 37.8 1.0 CD2 A:TYR128 4.1 41.5 1.0 HD2 A:TYR128 4.1 49.9 1.0 CG2 A:THR125 4.1 33.7 1.0 CA A:THR125 4.1 32.1 1.0 HG21 A:THR124 4.3 53.3 1.0 HD11 A:LEU446 4.3 89.7 1.0 O A:THR124 4.3 34.5 1.0 CG1 B:VAL283 4.4 47.2 1.0 HG21 B:VAL284 4.4 49.5 1.0 HG13 B:VAL284 4.4 45.6 1.0 HG23 A:THR125 4.4 40.5 1.0 CB B:VAL284 4.5 38.0 1.0 CD1 A:TYR128 4.5 46.2 1.0 N B:VAL284 4.5 36.9 1.0 O B:VAL283 4.6 36.7 1.0 N A:THR125 4.6 32.1 1.0 CB A:THR125 4.6 29.9 1.0 C A:THR124 4.6 36.9 1.0 C B:VAL283 4.7 37.9 1.0 HB A:THR125 4.7 35.9 1.0 HG11 B:VAL283 4.7 56.7 1.0 CD2 A:LEU446 4.7 79.4 1.0 HG21 A:THR125 4.7 40.5 1.0 HD1 A:TYR128 4.8 55.5 1.0 CE2 A:TYR128 4.8 44.8 1.0 HG13 B:VAL283 4.8 56.7 1.0 HB B:VAL283 4.9 49.9 1.0 CG1 B:VAL284 4.9 38.0 1.0 HD22 A:LEU446 5.0 95.3 1.0 H B:VAL284 5.0 44.3 1.0

Chlorine binding site 2 out of 3 in the M379A Mutant Tyrosine Phenol-Lyase Complexed with 3-Bromo-Dl- Phenylalanine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of M379A Mutant Tyrosine Phenol-Lyase Complexed with 3-Bromo-Dl- Phenylalanine within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl501 b:34.0 occ:1.00 HH22 C:ARG404 2.6 34.0 1.0 HH22 C:ARG381 2.8 38.6 1.0 HH12 C:ARG404 2.8 40.9 1.0 O C:HOH769 3.1 30.4 1.0 O C:HOH630 3.1 30.8 1.0 HE2 C:PHE448 3.2 36.7 1.0 HZ C:PHE36 3.2 30.6 1.0 HH12 C:ARG381 3.3 39.4 1.0 HZ C:PHE123 3.4 36.4 1.0 NH2 C:ARG404 3.4 28.3 1.0 NH2 C:ARG381 3.5 32.2 1.0 O D:HOH628 3.5 28.9 0.7 HE1 C:PHE449 3.6 30.3 1.0 NH1 C:ARG404 3.6 34.0 1.0 HE1 C:PHE123 3.7 38.6 1.0 O C:HOH971 3.8 33.4 1.0 NH1 C:ARG381 3.9 32.8 1.0 CE2 C:PHE448 4.0 30.6 1.0 HH21 C:ARG381 4.0 38.6 1.0 CZ C:ARG404 4.0 31.0 1.0 CZ C:PHE123 4.0 30.3 1.0 CZ C:PHE36 4.0 25.5 1.0 HH21 C:ARG404 4.1 34.0 1.0 HE1 C:PHE36 4.1 28.0 1.0 CZ C:ARG381 4.1 33.0 1.0 CE1 C:PHE123 4.2 32.1 1.0 CE1 C:PHE449 4.3 25.3 1.0 HZ C:PHE448 4.3 37.2 1.0 HH11 C:ARG404 4.3 40.9 1.0 HZ C:PHE449 4.4 32.6 1.0 CE1 C:PHE36 4.5 23.3 1.0 HB C:THR49 4.5 27.5 1.0 CZ C:PHE448 4.6 31.0 1.0 O C:HOH792 4.6 28.1 0.9 HH11 C:ARG381 4.6 39.4 1.0 CZ C:PHE449 4.7 27.2 1.0 HG1 C:THR49 4.8 26.6 1.0 CD2 C:PHE448 4.9 29.8 1.0 HD2 C:PHE448 4.9 35.8 1.0

Chlorine binding site 3 out of 3 in the M379A Mutant Tyrosine Phenol-Lyase Complexed with 3-Bromo-Dl- Phenylalanine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of M379A Mutant Tyrosine Phenol-Lyase Complexed with 3-Bromo-Dl- Phenylalanine within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl503 b:34.9 occ:1.00 HH22 D:ARG404 2.6 33.0 1.0 HH22 D:ARG381 2.7 39.6 1.0 HH12 D:ARG404 2.8 37.7 1.0 O D:HOH748 2.8 32.5 1.0 O D:HOH707 3.0 28.5 1.0 HE2 D:PHE448 3.1 33.2 1.0 HZ D:PHE36 3.2 34.0 1.0 HH12 D:ARG381 3.3 45.4 1.0 NH2 D:ARG404 3.4 27.5 1.0 NH2 D:ARG381 3.4 33.0 1.0 HZ D:PHE123 3.5 43.4 1.0 O C:HOH820 3.5 35.3 1.0 NH1 D:ARG404 3.5 31.4 1.0 HE1 D:PHE449 3.6 35.5 1.0 CE2 D:PHE448 3.9 27.7 1.0 NH1 D:ARG381 3.9 37.9 1.0 HH21 D:ARG381 3.9 39.6 1.0 CZ D:ARG404 3.9 30.1 1.0 HE1 D:PHE36 3.9 34.1 1.0 CZ D:PHE36 4.0 28.4 1.0 HZ D:PHE448 4.0 35.4 1.0 HE1 D:PHE123 4.0 44.4 1.0 HH21 D:ARG404 4.0 33.0 1.0 CZ D:ARG381 4.0 36.8 1.0 CZ D:PHE123 4.1 36.2 1.0 O D:HOH908 4.2 36.1 1.0 CE1 D:PHE449 4.2 29.6 1.0 HH11 D:ARG404 4.3 37.7 1.0 CZ D:PHE448 4.3 29.5 1.0 HZ D:PHE449 4.4 34.1 1.0 CE1 D:PHE36 4.4 28.4 1.0 CE1 D:PHE123 4.4 37.0 1.0 HB D:THR49 4.5 34.8 1.0 O D:HOH866 4.6 28.5 1.0 HG1 D:THR49 4.6 32.8 1.0 HH11 D:ARG381 4.6 45.4 1.0 CZ D:PHE449 4.7 28.4 1.0 CD2 D:PHE448 4.9 29.5 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