Magnesium in PDB 4bx3: Crystal Structure of Murine Chronophin (Pyridoxal Phosphate Phosphatase)

All present enzymatic activity of Crystal Structure of Murine Chronophin (Pyridoxal Phosphate Phosphatase):
3.1.3.3; 3.1.3.74;

The structure of Crystal Structure of Murine Chronophin (Pyridoxal Phosphate Phosphatase), PDB code: 4bx3 was solved by G.Knobloch, A.Gohla, H.Schindelin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.659 / 2.19
Space group	I 2 3
Cell size a, b, c (Å), α, β, γ (°)	167.100, 167.100, 167.100, 90.00, 90.00, 90.00
R / Rfree (%)	17.07 / 20.67

The binding sites of Magnesium atom in the Crystal Structure of Murine Chronophin (Pyridoxal Phosphate Phosphatase) (pdb code 4bx3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Murine Chronophin (Pyridoxal Phosphate Phosphatase), PDB code: 4bx3:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Murine Chronophin (Pyridoxal Phosphate Phosphatase)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Murine Chronophin (Pyridoxal Phosphate Phosphatase) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:32.1 occ:1.00 O A:HOH2010 2.0 35.5 1.0 O A:HOH2012 2.1 33.3 1.0 OD1 A:ASP234 2.1 33.0 1.0 O A:ASP27 2.2 31.2 1.0 OD2 A:ASP25 2.2 36.2 1.0 O A:HOH2011 2.3 32.3 1.0 CG A:ASP234 3.1 29.5 1.0 CG A:ASP25 3.3 28.3 1.0 OD2 A:ASP234 3.3 31.0 1.0 C A:ASP27 3.3 32.7 1.0 HB2 A:ASP27 3.6 41.2 1.0 HG21 A:VAL29 3.6 35.1 1.0 OD1 A:ASP25 3.7 28.7 1.0 HA3 A:GLY28 3.8 41.0 1.0 H A:ASP234 3.9 32.0 1.0 O A:HOH2072 4.1 48.9 1.0 OD2 A:ASP239 4.1 28.7 1.0 CA A:ASP27 4.2 29.5 1.0 H A:ASP27 4.3 35.0 1.0 N A:GLY28 4.3 39.3 1.0 CB A:ASP27 4.3 34.3 1.0 N A:ASP27 4.3 29.2 1.0 HB2 A:ARG235 4.3 42.0 1.0 O A:HOH2008 4.3 46.8 1.0 HB3 A:ASP25 4.4 33.9 1.0 CA A:GLY28 4.4 34.2 1.0 CB A:ASP234 4.4 27.7 1.0 CG2 A:VAL29 4.5 29.2 1.0 O A:HOH2009 4.5 26.0 1.0 CB A:ASP25 4.5 28.2 1.0 HG22 A:VAL29 4.5 35.1 1.0 HB3 A:ASP234 4.6 33.3 1.0 HB3 A:ASP27 4.7 41.2 1.0 N A:ASP234 4.7 26.6 1.0 HD2 A:ARG235 4.8 51.8 1.0 H A:CYS26 4.9 35.8 1.0 HG23 A:VAL29 4.9 35.1 1.0 H A:VAL29 4.9 32.8 1.0 C A:GLY28 4.9 30.9 1.0 C A:CYS26 4.9 34.1 1.0 HG21 A:VAL257 5.0 49.1 1.0 H A:ARG235 5.0 30.1 1.0 HB2 A:ASP25 5.0 33.9 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Murine Chronophin (Pyridoxal Phosphate Phosphatase)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Murine Chronophin (Pyridoxal Phosphate Phosphatase) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg302 b:45.3 occ:1.00 O B:HOH2005 2.1 41.9 1.0 O B:HOH2004 2.1 49.0 1.0 OD2 B:ASP25 2.2 50.2 1.0 OD1 B:ASP234 2.2 42.9 1.0 O B:HOH2006 2.3 40.3 1.0 O B:ASP27 2.4 37.2 1.0 CG B:ASP234 3.1 33.8 1.0 OD2 B:ASP234 3.3 36.7 1.0 C B:ASP27 3.4 39.4 1.0 CG B:ASP25 3.4 45.5 1.0 HB2 B:ASP27 3.5 42.7 1.0 O B:HOH2065 3.5 50.8 1.0 HA3 B:GLY28 3.7 44.4 1.0 HG21 B:VAL29 4.0 46.7 1.0 OD1 B:ASP25 4.0 36.9 1.0 H B:ASP234 4.0 42.8 1.0 HB2 B:ARG235 4.1 39.1 1.0 OD2 B:ASP239 4.2 34.4 1.0 CB B:ASP27 4.2 35.6 1.0 CA B:ASP27 4.2 34.4 1.0 N B:GLY28 4.3 35.9 1.0 HB3 B:ASP25 4.3 49.4 1.0 H B:ASP27 4.4 44.3 1.0 CA B:GLY28 4.4 37.0 1.0 HB3 B:ASP27 4.4 42.7 1.0 N B:ASP27 4.4 36.9 1.0 CB B:ASP234 4.5 36.3 1.0 O B:HOH2002 4.5 31.4 1.0 CB B:ASP25 4.5 41.2 1.0 O B:HOH2003 4.6 38.0 1.0 HB3 B:ASP234 4.6 43.6 1.0 HD2 B:ARG235 4.8 51.3 1.0 HB3 B:ARG235 4.8 39.1 1.0 N B:ASP234 4.8 35.6 1.0 HG21 B:VAL257 4.8 48.1 1.0 CG2 B:VAL29 4.9 38.9 1.0 O B:HOH2008 4.9 56.6 1.0 CB B:ARG235 4.9 32.5 1.0 HG22 B:VAL29 4.9 46.7 1.0 H B:CYS26 5.0 42.3 1.0

C.Kestler, G.Knobloch, I.Tessmer, E.Jeanclos, H.Schindelin, A.Gohla. Chronophin Dimerization Is Required For Proper Positioning of Its Substrate Specificity Loop. J.Biol.Chem. V. 289 3094 2014.
ISSN: ISSN 0021-9258
PubMed: 24338687
DOI: 10.1074/JBC.M113.536482