Chlorine in PDB 7mn9: PTP1B 1-284 F225Y-R199N

All present enzymatic activity of PTP1B 1-284 F225Y-R199N:
3.1.3.48;

The structure of PTP1B 1-284 F225Y-R199N, PDB code: 7mn9 was solved by K.R.Torgeson, R.Page, W.Peti, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.31 / 1.24
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	88.464, 88.464, 72.429, 90, 90, 120
R / Rfree (%)	16.2 / 18

The binding sites of Chlorine atom in the PTP1B 1-284 F225Y-R199N (pdb code 7mn9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the PTP1B 1-284 F225Y-R199N, PDB code: 7mn9:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the PTP1B 1-284 F225Y-R199N


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of PTP1B 1-284 F225Y-R199N within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl305 b:25.7 occ:1.00 O A:HOH748 3.0 47.4 1.0 N A:LYS39 3.3 17.1 1.0 CD A:PRO38 3.6 18.4 1.0 CG A:LYS39 3.6 21.6 1.0 CB A:LYS39 3.6 19.5 1.0 N A:PRO38 3.7 17.5 1.0 CB A:LEU37 3.9 17.1 1.0 CD A:LYS39 4.0 26.8 1.0 CB A:PRO38 4.0 20.5 1.0 CA A:LYS39 4.1 18.6 1.0 CG A:PRO38 4.2 22.0 1.0 CA A:PRO38 4.2 19.1 1.0 C A:PRO38 4.2 18.6 1.0 C A:LEU37 4.3 16.2 1.0 CD2 A:LEU37 4.4 19.9 1.0 CA A:LEU37 4.6 16.2 1.0 CG A:LEU37 4.6 18.3 1.0 CE A:LYS39 4.6 35.3 1.0 CD1 A:LEU37 4.7 20.1 1.0

Chlorine binding site 2 out of 2 in the PTP1B 1-284 F225Y-R199N


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of PTP1B 1-284 F225Y-R199N within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl306 b:28.5 occ:1.00 NH2 A:ARG254 3.2 17.8 1.0 NH1 A:ARG254 3.3 18.0 1.0 NE A:ARG24 3.4 44.2 1.0 NE2 A:GLN262 3.5 21.4 0.7 O A:HOH624 3.6 34.3 1.0 CZ A:ARG254 3.6 16.5 1.0 CA A:GLY259 3.8 15.5 1.0 CG A:ARG24 3.9 24.8 1.0 OH A:TYR20 3.9 23.5 1.0 CD A:ARG24 4.0 34.1 1.0 O A:HOH686 4.0 40.2 1.0 CZ A:ARG24 4.3 66.7 1.0 NH2 A:ARG24 4.4 72.5 1.0 C A:GLY259 4.5 15.3 1.0 O A:GLY259 4.5 16.9 1.0 N A:GLY259 4.6 14.4 1.0 CB A:ARG24 4.7 25.0 1.0 O A:ILE261 4.7 17.8 1.0 O A:HOH565 4.7 16.3 1.0 O A:HOH650 4.7 60.0 1.0 CD A:GLN262 4.8 25.0 0.7 O A:HOH733 4.8 39.8 1.0 CZ A:TYR20 4.9 20.9 1.0 NE A:ARG254 4.9 15.8 1.0

K.R.Torgeson, M.W.Clarkson, D.Granata, K.Lindorff-Larsen, R.Page, W.Peti. Conserved Conformational Dynamics Determine Enzyme Activity. Sci Adv V. 8 O5546 2022.
ISSN: ESSN 2375-2548
PubMed: 35921420
DOI: 10.1126/SCIADV.ABO5546