Chlorine in PDB 2b4p: Structure of the D223N Mutant of Selenomonas Ruminantium Ptp-Like Phytase

All present enzymatic activity of Structure of the D223N Mutant of Selenomonas Ruminantium Ptp-Like Phytase:
3.1.3.72;

The structure of Structure of the D223N Mutant of Selenomonas Ruminantium Ptp-Like Phytase, PDB code: 2b4p was solved by R.J.Gruninger, L.B.Selinger, S.C.Mosimann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 1.81
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	46.200, 137.420, 79.610, 90.00, 102.58, 90.00
R / Rfree (%)	19.6 / 21.4

The binding sites of Chlorine atom in the Structure of the D223N Mutant of Selenomonas Ruminantium Ptp-Like Phytase (pdb code 2b4p). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of the D223N Mutant of Selenomonas Ruminantium Ptp-Like Phytase, PDB code: 2b4p:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structure of the D223N Mutant of Selenomonas Ruminantium Ptp-Like Phytase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of the D223N Mutant of Selenomonas Ruminantium Ptp-Like Phytase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl353 b:17.0 occ:1.00 O B:HOH557 3.0 28.2 1.0 O B:HOH603 3.1 15.0 1.0 N B:GLN161 3.2 13.1 1.0 O B:HOH615 3.4 19.3 1.0 CB B:GLN161 3.9 12.9 1.0 CA B:SER160 4.0 13.2 1.0 CB B:SER160 4.0 13.1 1.0 C B:SER160 4.1 13.1 1.0 CA B:GLN161 4.2 13.3 1.0 CG B:GLU230 4.3 15.1 1.0 O B:HOH391 4.4 12.6 1.0 CB B:GLU230 4.8 13.7 1.0 OE1 B:GLU230 4.9 16.9 1.0

Chlorine binding site 2 out of 2 in the Structure of the D223N Mutant of Selenomonas Ruminantium Ptp-Like Phytase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of the D223N Mutant of Selenomonas Ruminantium Ptp-Like Phytase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl961 b:15.0 occ:1.00 O B:HOH607 3.0 17.0 1.0 OG1 B:THR333 3.2 14.2 1.0 CG2 B:THR333 3.7 14.0 1.0 CB B:THR333 3.8 14.3 1.0 CG1 B:VAL337 4.0 14.5 1.0 CA B:THR333 4.0 14.2 1.0 CD B:PRO334 4.1 13.4 1.0 CB B:VAL337 4.5 14.5 1.0 O B:GLN332 4.5 15.5 1.0 CG2 B:VAL337 4.5 14.7 1.0 N B:PRO334 5.0 13.6 1.0 N B:THR333 5.0 14.8 1.0

A.A.Puhl, R.J.Gruninger, R.Greiner, T.W.Janzen, S.C.Mosimann, L.B.Selinger. Kinetic and Structural Analysis of A Bacterial Protein Tyrosine Phosphatase-Like Myo-Inositol Polyphosphatase. Protein Sci. V. 16 1368 2007.
ISSN: ISSN 0961-8368
PubMed: 17567745
DOI: 10.1110/PS.062738307