Chlorine in PDB 4zrt: PTP1BC215S Bound to Nephrin Peptide Substrate

All present enzymatic activity of PTP1BC215S Bound to Nephrin Peptide Substrate:
3.1.3.48;

The structure of PTP1BC215S Bound to Nephrin Peptide Substrate, PDB code: 4zrt was solved by N.G.Selner, C.E.Bell, D.Pei, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.95 / 1.74
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	43.848, 88.725, 50.043, 90.00, 97.25, 90.00
R / Rfree (%)	16.8 / 20.7

The structure of PTP1BC215S Bound to Nephrin Peptide Substrate also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Chlorine atom in the PTP1BC215S Bound to Nephrin Peptide Substrate (pdb code 4zrt). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the PTP1BC215S Bound to Nephrin Peptide Substrate, PDB code: 4zrt:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the PTP1BC215S Bound to Nephrin Peptide Substrate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of PTP1BC215S Bound to Nephrin Peptide Substrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:35.1 occ:1.00 O A:HOH663 3.2 43.3 1.0 N A:LYS39 3.3 18.7 1.0 CD A:PRO38 3.6 21.1 1.0 CB A:LYS39 3.6 21.7 1.0 CG A:LYS39 3.7 28.7 1.0 N A:PRO38 3.7 17.2 1.0 CD A:LYS39 3.9 32.6 1.0 CB A:LEU37 3.9 17.3 1.0 CG A:PRO38 4.0 20.2 1.0 CA A:LYS39 4.1 21.9 1.0 CB A:PRO38 4.2 20.3 1.0 C A:PRO38 4.2 16.4 1.0 CE A:LYS39 4.2 38.2 1.0 C A:LEU37 4.2 17.0 1.0 CA A:PRO38 4.3 17.9 1.0 CD2 A:LEU37 4.4 21.1 1.0 CA A:LEU37 4.5 15.8 1.0 CG A:LEU37 4.6 19.0 1.0 CD1 A:LEU37 4.8 17.4 1.0

Chlorine binding site 2 out of 2 in the PTP1BC215S Bound to Nephrin Peptide Substrate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of PTP1BC215S Bound to Nephrin Peptide Substrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl304 b:21.5 occ:1.00 O A:HOH520 3.0 18.2 1.0 O A:HOH646 3.1 37.3 1.0 N A:VAL113 3.2 14.1 1.0 O A:HOH575 3.4 28.4 1.0 CE1 A:HIS175 3.6 16.4 1.0 CA A:ARG112 3.7 14.5 1.0 CG2 A:VAL113 3.7 19.9 1.0 CG1 A:VAL113 3.9 15.8 1.0 CB A:ARG112 3.9 16.9 1.0 C A:ARG112 4.0 13.3 1.0 NE2 A:HIS175 4.1 15.9 1.0 CB A:VAL113 4.1 15.8 1.0 O A:HOH481 4.2 37.8 1.0 CG A:ARG112 4.2 22.7 1.0 CA A:VAL113 4.2 14.8 1.0 CH2 A:TRP125 4.4 11.6 1.0 O A:HOH617 4.5 30.5 1.0 CE A:MET109 4.6 16.0 1.0 ND1 A:HIS175 4.8 14.5 1.0 CZ2 A:TRP125 4.9 11.8 1.0 O A:ASN111 4.9 13.2 1.0 N A:ARG112 5.0 15.1 1.0

N.G.Selner, R.Luechapanichkul, X.Chen, B.G.Neel, Z.Y.Zhang, S.Knapp, C.E.Bell, D.Pei. Diverse Levels of Sequence Selectivity and Catalytic Efficiency of Protein-Tyrosine Phosphatases. Biochemistry V. 53 397 2014.
ISSN: ISSN 0006-2960
PubMed: 24359314
DOI: 10.1021/BI401223R