Chlorine in PDB 7mov: PTP1B 1-301 F225Y-R199N Mutations

All present enzymatic activity of PTP1B 1-301 F225Y-R199N Mutations:
3.1.3.48;

The structure of PTP1B 1-301 F225Y-R199N Mutations, PDB code: 7mov 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)	37.82 / 1.65
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	114.359, 90.102, 74.49, 90, 110.93, 90
R / Rfree (%)	16.5 / 19.3

The binding sites of Chlorine atom in the PTP1B 1-301 F225Y-R199N Mutations (pdb code 7mov). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the PTP1B 1-301 F225Y-R199N Mutations, PDB code: 7mov:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the PTP1B 1-301 F225Y-R199N Mutations


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of PTP1B 1-301 F225Y-R199N Mutations within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl404 b:45.0 occ:1.00 NH2 A:ARG254 3.2 24.4 1.0 NH1 A:ARG254 3.2 24.6 1.0 NE2 A:GLN262 3.4 24.9 0.6 CZ A:ARG254 3.6 25.7 1.0 NE A:ARG24 3.6 53.8 1.0 O A:HOH601 3.7 42.0 1.0 O A:HOH723 3.8 47.7 1.0 O A:HOH687 3.8 54.1 1.0 CA A:GLY259 3.8 23.4 1.0 OH A:TYR20 3.9 29.3 1.0 CG A:ARG24 4.0 40.3 1.0 CD A:ARG24 4.0 46.1 1.0 O A:HOH697 4.3 57.6 1.0 CZ A:ARG24 4.4 65.7 1.0 O A:GLY259 4.5 22.6 1.0 C A:GLY259 4.5 23.8 1.0 CB A:ARG24 4.6 38.9 1.0 O A:HOH629 4.7 21.7 1.0 N A:GLY259 4.7 20.6 1.0 O A:ILE261 4.7 27.2 1.0 CD A:GLN262 4.7 26.1 0.6 NH2 A:ARG24 4.8 72.8 1.0 CZ A:TYR20 4.8 31.5 1.0 NE A:ARG254 4.9 21.9 1.0

Chlorine binding site 2 out of 3 in the PTP1B 1-301 F225Y-R199N Mutations


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of PTP1B 1-301 F225Y-R199N Mutations within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl405 b:29.9 occ:1.00 OG A:SER216 2.9 21.3 0.8 NZ A:LYS120 3.1 30.9 1.0 O A:HOH675 3.2 30.1 1.0 N A:SER216 3.4 20.3 1.0 CB A:SER216 3.5 22.1 0.8 NE A:ARG221 3.6 20.9 1.0 CZ A:ARG221 3.7 22.0 1.0 CB A:CYS215 3.7 20.5 1.0 CE A:LYS120 3.7 33.8 1.0 CD A:LYS120 3.7 29.2 1.0 CB A:SER216 3.7 23.1 0.2 CD A:ARG221 3.7 18.7 1.0 NH1 A:ARG221 3.9 20.4 1.0 CA A:SER216 4.1 21.9 0.8 NH2 A:ARG221 4.1 27.3 1.0 CA A:SER216 4.1 21.9 0.2 CB A:ASN111 4.2 19.5 1.0 C A:CYS215 4.3 24.2 1.0 CG A:ARG221 4.3 21.4 1.0 O A:HOH515 4.4 40.4 1.0 SG A:CYS215 4.4 20.9 1.0 O A:HOH670 4.4 32.6 1.0 CA A:CYS215 4.4 21.3 1.0 O A:HOH580 4.7 41.1 1.0 O A:HOH614 4.8 22.6 1.0 CG A:ASN111 4.9 25.6 1.0 CB A:ARG221 4.9 19.6 1.0 CG A:LYS120 5.0 32.2 1.0

Chlorine binding site 3 out of 3 in the PTP1B 1-301 F225Y-R199N Mutations


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of PTP1B 1-301 F225Y-R199N Mutations within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl406 b:29.4 occ:1.00 N A:LYS39 3.3 23.4 1.0 CD A:PRO38 3.7 23.1 1.0 CB A:LYS39 3.7 24.5 1.0 N A:PRO38 3.8 22.8 1.0 CG A:LYS39 3.8 25.1 1.0 CB A:PRO38 3.9 27.4 1.0 CA A:LYS39 4.1 22.5 1.0 CD A:LYS39 4.1 31.0 1.0 CB A:LEU37 4.2 20.9 1.0 C A:PRO38 4.2 22.5 1.0 CA A:PRO38 4.2 21.5 1.0 CG A:PRO38 4.2 29.4 1.0 C A:LEU37 4.4 20.6 1.0 CA A:LEU37 4.7 22.7 1.0 CE A:LYS39 4.8 37.3 1.0 CD2 A:LEU37 4.8 22.6 1.0 CG A:LEU37 5.0 22.5 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