Chlorine in PDB 6byf: Crystal Structure of the Core Catalytic Domain of Pp-Ip Phosphatase SIW14 From S. Cerevisiae in Complex with Citrate

All present enzymatic activity of Crystal Structure of the Core Catalytic Domain of Pp-Ip Phosphatase SIW14 From S. Cerevisiae in Complex with Citrate:
3.1.3.48;

The structure of Crystal Structure of the Core Catalytic Domain of Pp-Ip Phosphatase SIW14 From S. Cerevisiae in Complex with Citrate, PDB code: 6byf was solved by H.Wang, S.B.Shears, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.45 / 2.35
Space group	P 65 2 2 1
Cell size a, b, c (Å), α, β, γ (°)	92.968, 92.968, 814.716, 90.00, 90.00, 120.00
R / Rfree (%)	20.6 / 22.9

The binding sites of Chlorine atom in the Crystal Structure of the Core Catalytic Domain of Pp-Ip Phosphatase SIW14 From S. Cerevisiae in Complex with Citrate (pdb code 6byf). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of the Core Catalytic Domain of Pp-Ip Phosphatase SIW14 From S. Cerevisiae in Complex with Citrate, PDB code: 6byf:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of the Core Catalytic Domain of Pp-Ip Phosphatase SIW14 From S. Cerevisiae in Complex with Citrate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the Core Catalytic Domain of Pp-Ip Phosphatase SIW14 From S. Cerevisiae in Complex with Citrate within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl303 b:44.4 occ:1.00 NE2 D:GLN232 3.1 42.4 1.0 NE1 D:TRP281 3.2 47.3 1.0 O D:HOH409 3.3 50.6 1.0 NE1 D:TRP234 3.4 35.5 1.0 NE C:ARG146 3.5 57.9 1.0 CE1 C:PHE142 3.7 37.6 1.0 CE2 D:TRP281 4.0 41.2 1.0 CD C:ARG146 4.1 45.5 1.0 CD1 D:TRP234 4.2 35.9 1.0 CG1 C:VAL116 4.2 46.5 1.0 CZ2 D:TRP281 4.2 42.7 1.0 CG C:ARG146 4.2 46.2 1.0 CD1 D:TRP281 4.2 45.1 1.0 CB D:GLN232 4.2 40.2 1.0 CD D:GLN232 4.2 39.8 1.0 CD1 C:PHE142 4.3 42.9 1.0 CB C:ARG146 4.4 45.4 1.0 CZ C:ARG146 4.4 64.1 1.0 NH2 C:ARG146 4.5 56.7 1.0 CE2 D:TRP234 4.5 33.0 1.0 CG D:GLN232 4.5 35.1 1.0 O D:GLN232 4.7 39.8 1.0 CZ C:PHE142 4.8 42.0 1.0 CZ2 D:TRP234 4.9 38.0 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of the Core Catalytic Domain of Pp-Ip Phosphatase SIW14 From S. Cerevisiae in Complex with Citrate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of the Core Catalytic Domain of Pp-Ip Phosphatase SIW14 From S. Cerevisiae in Complex with Citrate within 5.0Å range: probe atom residue distance (Å) B Occ G:Cl302 b:41.4 occ:1.00 NE G:ARG146 3.2 59.9 1.0 CE1 G:PHE142 3.7 33.2 1.0 CG G:ARG146 3.9 42.4 1.0 NH2 G:ARG146 3.9 58.4 1.0 CZ G:ARG146 4.0 60.1 1.0 CD G:ARG146 4.0 46.1 1.0 CD1 G:PHE142 4.0 38.7 1.0 CB G:ARG146 4.1 40.7 1.0 CG1 G:VAL116 4.3 44.8 1.0 CZ G:PHE142 4.9 36.6 1.0

H.Wang, C.Gu, R.J.Rolfes, H.J.Jessen, S.B.Shears. Structural and Biochemical Characterization of SIW14: A Protein-Tyrosine Phosphatase Fold That Metabolizes Inositol Pyrophosphates. J. Biol. Chem. V. 293 6905 2018.
ISSN: ESSN 1083-351X
PubMed: 29540476
DOI: 10.1074/JBC.RA117.001670