Chlorine in PDB 4nyh: Orthorhombic Crystal Form of PIR1 Dual Specificity Phosphatase Core

The structure of Orthorhombic Crystal Form of PIR1 Dual Specificity Phosphatase Core, PDB code: 4nyh was solved by R.S.Sankhala, R.K.Lokareddy, G.Cingolani, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 1.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.026, 62.723, 178.773, 90.00, 90.00, 90.00
R / Rfree (%)	13.7 / 17

The binding sites of Chlorine atom in the Orthorhombic Crystal Form of PIR1 Dual Specificity Phosphatase Core (pdb code 4nyh). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Orthorhombic Crystal Form of PIR1 Dual Specificity Phosphatase Core, PDB code: 4nyh:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Orthorhombic Crystal Form of PIR1 Dual Specificity Phosphatase Core


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Orthorhombic Crystal Form of PIR1 Dual Specificity Phosphatase Core within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:13.2 occ:1.00 H A:TYR95 2.2 13.3 1.0 H A:THR96 2.4 13.4 1.0 HH12 A:ARG158 2.5 13.5 1.0 HH22 A:ARG158 2.6 13.0 1.0 HG23 A:THR96 2.8 15.7 1.0 HA A:THR94 2.9 12.3 1.0 HB A:THR94 3.0 12.2 1.0 HG1 A:THR153 3.1 15.2 1.0 N A:TYR95 3.2 12.7 1.0 O A:HOH554 3.2 40.6 1.0 OG1 A:THR96 3.2 17.6 1.0 OG1 A:THR153 3.3 15.6 1.0 NH1 A:ARG158 3.3 13.6 1.0 HG1 A:THR96 3.3 17.2 1.0 N A:THR96 3.4 13.2 1.0 NH2 A:ARG158 3.4 13.0 1.0 O A:HOH558 3.5 33.6 1.0 CG2 A:THR96 3.5 15.5 1.0 HE1 A:TYR99 3.6 19.6 1.0 HG22 A:THR94 3.6 12.8 1.0 CA A:THR94 3.6 12.0 1.0 HG21 A:THR96 3.6 15.8 1.0 CB A:THR94 3.6 12.3 1.0 HD2 A:TYR95 3.7 14.7 1.0 CD2 A:TYR95 3.7 15.2 1.0 CZ A:ARG158 3.8 11.6 1.0 CB A:THR96 3.8 14.6 1.0 CE2 A:TYR95 3.8 14.3 1.0 C A:THR94 3.9 12.5 1.0 HE2 A:TYR95 3.9 14.6 1.0 HH11 A:ARG158 4.0 13.2 1.0 HH A:TYR99 4.0 27.5 1.0 HH21 A:ARG158 4.1 12.7 1.0 CG2 A:THR94 4.1 12.4 1.0 CA A:TYR95 4.2 13.2 1.0 CA A:THR96 4.2 13.0 1.0 C A:TYR95 4.3 13.2 1.0 CG A:TYR95 4.3 13.8 1.0 HG22 A:THR96 4.3 15.6 1.0 O A:HOH551 4.4 39.2 1.0 HG21 A:THR94 4.5 12.5 1.0 CE1 A:TYR99 4.5 21.0 1.0 CZ A:TYR95 4.5 15.1 1.0 CB A:THR153 4.7 14.3 1.0 HB A:THR96 4.7 14.4 1.0 HA A:THR96 4.7 13.2 1.0 OH A:TYR99 4.7 32.3 1.0 H A:GLN97 4.7 13.9 1.0 H A:THR153 4.8 11.2 1.0 CB A:TYR95 4.8 13.7 1.0 OG1 A:THR94 4.9 12.5 1.0 N A:THR94 4.9 11.3 1.0 HG23 A:THR94 4.9 12.7 1.0 CD1 A:TYR95 4.9 13.5 1.0 HB A:THR153 4.9 14.8 1.0 HA A:TYR95 5.0 13.9 1.0

Chlorine binding site 2 out of 3 in the Orthorhombic Crystal Form of PIR1 Dual Specificity Phosphatase Core


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Orthorhombic Crystal Form of PIR1 Dual Specificity Phosphatase Core within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl302 b:13.9 occ:1.00 H B:TYR95 2.2 13.4 1.0 H B:THR96 2.5 14.2 1.0 HH12 B:ARG158 2.5 13.9 1.0 HG23 B:THR96 2.6 19.0 1.0 HH22 B:ARG158 2.7 13.6 1.0 HA B:THR94 2.9 12.3 1.0 HB B:THR94 3.0 13.7 1.0 HG1 B:THR153 3.1 17.1 1.0 N B:TYR95 3.2 13.3 1.0 OG1 B:THR96 3.2 25.7 1.0 HG1 B:THR96 3.2 23.3 1.0 OG1 B:THR153 3.3 17.0 1.0 NH1 B:ARG158 3.3 14.0 1.0 CG2 B:THR96 3.3 18.6 1.0 N B:THR96 3.4 14.3 1.0 O B:HOH624 3.4 39.2 1.0 NH2 B:ARG158 3.4 13.6 1.0 HG21 B:THR96 3.4 18.4 1.0 O B:HOH669 3.5 36.9 1.0 HG22 B:THR94 3.6 14.7 1.0 CA B:THR94 3.6 12.1 1.0 HD2 B:TYR95 3.6 15.1 1.0 CB B:THR94 3.7 13.1 1.0 CD2 B:TYR95 3.7 15.5 1.0 CB B:THR96 3.7 18.8 1.0 HE1 B:TYR99 3.8 22.4 1.0 CE2 B:TYR95 3.8 15.2 1.0 CZ B:ARG158 3.8 13.0 1.0 HE2 B:TYR95 3.8 16.0 1.0 C B:THR94 3.9 12.6 1.0 HH11 B:ARG158 4.0 13.6 1.0 CG2 B:THR94 4.1 14.9 1.0 HH21 B:ARG158 4.1 13.2 1.0 HG22 B:THR96 4.2 18.9 1.0 CA B:THR96 4.2 15.6 1.0 CA B:TYR95 4.2 14.0 1.0 C B:TYR95 4.3 14.0 1.0 CG B:TYR95 4.3 14.4 1.0 HH B:TYR99 4.3 24.9 1.0 HG21 B:THR94 4.5 14.8 1.0 CZ B:TYR95 4.5 19.2 1.0 HB B:THR96 4.6 18.6 1.0 CE1 B:TYR99 4.7 22.2 1.0 HA B:THR96 4.7 15.9 1.0 CB B:THR153 4.7 13.8 1.0 H B:GLN97 4.8 18.9 1.0 H B:THR153 4.8 13.0 1.0 CB B:TYR95 4.8 14.4 1.0 CD1 B:TYR95 4.9 15.7 1.0 N B:THR94 4.9 12.5 1.0 OG1 B:THR94 4.9 13.9 1.0 HG23 B:THR94 4.9 14.4 1.0 CE1 B:TYR95 4.9 18.0 1.0 HB B:THR153 5.0 14.5 1.0

Chlorine binding site 3 out of 3 in the Orthorhombic Crystal Form of PIR1 Dual Specificity Phosphatase Core


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Orthorhombic Crystal Form of PIR1 Dual Specificity Phosphatase Core within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl302 b:15.2 occ:1.00 H C:TYR95 2.2 13.9 1.0 HH12 C:ARG158 2.5 15.3 1.0 H C:THR96 2.6 14.5 1.0 HG23 C:THR96 2.6 17.0 1.0 HH22 C:ARG158 2.8 15.1 1.0 HA C:THR94 2.9 15.4 1.0 HB C:THR94 3.0 15.2 1.0 HG1 C:THR153 3.1 17.9 1.0 O C:HOH497 3.2 59.2 1.0 N C:TYR95 3.2 13.7 1.0 NH1 C:ARG158 3.3 14.9 1.0 OG1 C:THR153 3.3 18.0 1.0 O C:HOH431 3.3 27.3 1.0 OG1 C:THR96 3.4 27.0 1.0 CG2 C:THR96 3.4 16.2 1.0 HG1 C:THR96 3.4 23.5 1.0 N C:THR96 3.4 14.5 1.0 HG21 C:THR96 3.5 16.6 1.0 NH2 C:ARG158 3.5 14.2 1.0 HD2 C:TYR95 3.5 16.7 1.0 HG22 C:THR94 3.6 16.8 1.0 CA C:THR94 3.6 15.0 1.0 CD2 C:TYR95 3.6 16.0 1.0 CB C:THR94 3.6 15.3 1.0 CE2 C:TYR95 3.7 17.1 1.0 HE2 C:TYR95 3.7 17.4 1.0 CB C:THR96 3.8 19.0 1.0 CZ C:ARG158 3.9 13.5 1.0 C C:THR94 3.9 14.7 1.0 HE1 C:TYR99 3.9 22.7 1.0 HH11 C:ARG158 3.9 14.4 1.0 CG2 C:THR94 4.1 16.4 1.0 HG22 C:THR96 4.2 17.8 1.0 CA C:TYR95 4.2 14.8 1.0 CA C:THR96 4.2 15.8 1.0 HH21 C:ARG158 4.2 14.7 1.0 CG C:TYR95 4.3 16.2 1.0 C C:TYR95 4.3 13.7 1.0 HH C:TYR99 4.3 25.9 1.0 CZ C:TYR95 4.4 17.7 1.0 HG21 C:THR94 4.5 16.2 1.0 HA C:THR96 4.7 16.2 1.0 HB C:THR96 4.7 18.8 1.0 CB C:THR153 4.7 15.2 1.0 CB C:TYR95 4.8 16.7 1.0 CE1 C:TYR99 4.8 23.3 1.0 CD1 C:TYR95 4.8 15.9 1.0 H C:THR153 4.9 14.6 1.0 N C:THR94 4.9 15.3 1.0 OG1 C:THR94 4.9 16.4 1.0 HG23 C:THR94 4.9 16.6 1.0 CE1 C:TYR95 4.9 17.7 1.0 H C:GLN97 4.9 17.3 1.0

R.S.Sankhala, R.K.Lokareddy, G.Cingolani. Structure of Human PIR1, An Atypical Dual-Specificity Phosphatase. Biochemistry V. 53 862 2014.
ISSN: ISSN 0006-2960
PubMed: 24447265
DOI: 10.1021/BI401240X