Chlorine in PDB 5ka9: Protein Tyrosine Phosphatase 1B L192A Mutant in Complex with TCS401, Open State

All present enzymatic activity of Protein Tyrosine Phosphatase 1B L192A Mutant in Complex with TCS401, Open State:
3.1.3.48;

The structure of Protein Tyrosine Phosphatase 1B L192A Mutant in Complex with TCS401, Open State, PDB code: 5ka9 was solved by M.S.Choy, W.Peti, R.Page, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.36 / 2.07
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	88.709, 88.709, 106.218, 90.00, 90.00, 120.00
R / Rfree (%)	18.9 / 23

The binding sites of Chlorine atom in the Protein Tyrosine Phosphatase 1B L192A Mutant in Complex with TCS401, Open State (pdb code 5ka9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Protein Tyrosine Phosphatase 1B L192A Mutant in Complex with TCS401, Open State, PDB code: 5ka9:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Protein Tyrosine Phosphatase 1B L192A Mutant in Complex with TCS401, Open State


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Protein Tyrosine Phosphatase 1B L192A Mutant in Complex with TCS401, Open State within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:27.9 occ:1.00 N A:VAL113 3.1 17.6 1.0 O A:HOH454 3.2 25.1 1.0 O A:HOH547 3.3 25.9 1.0 CE1 A:HIS175 3.6 21.0 1.0 CA A:ARG112 3.6 17.9 1.0 CB A:ARG112 3.8 25.1 1.0 CG2 A:VAL113 3.8 18.3 1.0 C A:ARG112 3.9 20.5 1.0 CB A:VAL113 3.9 21.1 1.0 CA A:VAL113 4.1 22.0 1.0 CG A:ARG112 4.1 20.6 1.0 NE2 A:HIS175 4.1 21.7 1.0 O A:HOH458 4.3 37.4 1.0 O A:HOH567 4.3 29.4 1.0 CH2 A:TRP125 4.4 22.6 1.0 O A:HOH564 4.5 42.1 1.0 CE A:MET109 4.6 15.9 1.0 ND1 A:HIS175 4.7 21.6 1.0 O A:ASN111 4.8 18.6 1.0 CZ2 A:TRP125 4.9 20.2 1.0 O A:HOH582 4.9 33.9 1.0 N A:ARG112 4.9 20.1 1.0

Chlorine binding site 2 out of 4 in the Protein Tyrosine Phosphatase 1B L192A Mutant in Complex with TCS401, Open State


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Protein Tyrosine Phosphatase 1B L192A Mutant in Complex with TCS401, Open State within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl303 b:41.2 occ:1.00 NE A:ARG24 3.2 40.1 1.0 NH1 A:ARG254 3.3 24.0 1.0 NH2 A:ARG254 3.4 25.1 1.0 O A:HOH518 3.5 34.2 1.0 OE1 A:GLN262 3.6 27.2 1.0 CZ A:ARG254 3.8 26.4 1.0 CA A:GLY259 3.8 21.7 1.0 OH A:TYR20 3.9 28.9 1.0 CD A:ARG24 3.9 36.0 1.0 CG A:ARG24 4.0 34.8 1.0 O A:HOH544 4.0 40.9 1.0 NH2 A:ARG24 4.1 60.0 1.0 CZ A:ARG24 4.1 53.1 1.0 O A:GLY259 4.5 21.1 1.0 C A:GLY259 4.5 24.7 1.0 CB A:ARG24 4.7 32.0 1.0 CD A:GLN262 4.7 27.3 1.0 O A:ILE261 4.7 21.7 1.0 N A:GLY259 4.7 20.4 1.0 CZ A:TYR20 4.8 27.3 1.0 O A:HOH499 4.9 20.5 1.0

Chlorine binding site 3 out of 4 in the Protein Tyrosine Phosphatase 1B L192A Mutant in Complex with TCS401, Open State


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Protein Tyrosine Phosphatase 1B L192A Mutant in Complex with TCS401, Open State within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl304 b:45.5 occ:1.00 N A:LYS39 3.3 29.8 1.0 CG A:LYS39 3.5 29.9 1.0 CD A:PRO38 3.6 30.4 1.0 CB A:LYS39 3.6 27.2 1.0 N A:PRO38 3.7 38.0 1.0 CB A:LEU37 3.9 27.2 1.0 CD A:LYS39 4.0 28.4 1.0 CA A:LYS39 4.1 32.5 1.0 CB A:PRO38 4.1 38.8 1.0 CG A:PRO38 4.2 35.8 1.0 C A:PRO38 4.2 27.3 1.0 C A:LEU37 4.3 34.9 1.0 CA A:PRO38 4.3 33.7 1.0 CD2 A:LEU37 4.4 27.5 1.0 CA A:LEU37 4.5 23.3 1.0 CG A:LEU37 4.6 29.5 1.0 CD1 A:LEU37 4.8 23.8 1.0 CE A:LYS39 4.8 37.7 1.0

Chlorine binding site 4 out of 4 in the Protein Tyrosine Phosphatase 1B L192A Mutant in Complex with TCS401, Open State


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Protein Tyrosine Phosphatase 1B L192A Mutant in Complex with TCS401, Open State within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl305 b:43.9 occ:1.00 NH1 A:ARG238 3.1 32.6 1.0 N A:ASP245 3.1 29.7 1.0 NH2 A:ARG238 3.5 37.9 1.0 CB A:ASP245 3.6 28.5 1.0 O A:ASP245 3.7 29.6 1.0 CZ A:ARG238 3.8 37.1 1.0 CA A:ASP245 3.8 31.7 1.0 C A:VAL244 4.1 33.2 1.0 CB A:LYS248 4.1 29.8 1.0 C A:ASP245 4.2 29.6 1.0 CD A:LYS248 4.2 55.2 1.0 CA A:VAL244 4.2 35.9 1.0 CG2 A:VAL249 4.2 25.0 1.0 CG1 A:VAL244 4.6 33.0 1.0 O A:SER243 4.8 43.5 1.0 CG A:LYS248 4.8 40.1 1.0 CG A:ASP245 4.9 40.2 1.0 O A:HOH583 4.9 42.8 1.0 CB A:VAL244 5.0 38.0 1.0 N A:VAL249 5.0 21.0 1.0

M.S.Choy, Y.Li, L.E.Machado, M.B.Kunze, C.R.Connors, X.Wei, K.Lindorff-Larsen, R.Page, W.Peti. Conformational Rigidity and Protein Dynamics at Distinct Timescales Regulate PTP1B Activity and Allostery. Mol. Cell V. 65 644 2017.
ISSN: ISSN 1097-4164
PubMed: 28212750
DOI: 10.1016/J.MOLCEL.2017.01.014