Magnesium in PDB 4uau: Crystal Structure of Cbby (Mutant D10N) From Rhodobacter Sphaeroides in Complex with Xylulose-(1,5)Bisphosphate, Crystal Form II

The structure of Crystal Structure of Cbby (Mutant D10N) From Rhodobacter Sphaeroides in Complex with Xylulose-(1,5)Bisphosphate, Crystal Form II, PDB code: 4uau was solved by A.Bracher, A.Sharma, A.Starling-Windhof, F.U.Hartl, M.Hayer-Hartl, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.288, 69.767, 125.793, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 21.1

The binding sites of Magnesium atom in the Crystal Structure of Cbby (Mutant D10N) From Rhodobacter Sphaeroides in Complex with Xylulose-(1,5)Bisphosphate, Crystal Form II (pdb code 4uau). 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 Cbby (Mutant D10N) From Rhodobacter Sphaeroides in Complex with Xylulose-(1,5)Bisphosphate, Crystal Form II, PDB code: 4uau:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Cbby (Mutant D10N) From Rhodobacter Sphaeroides in Complex with Xylulose-(1,5)Bisphosphate, Crystal Form II


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 Cbby (Mutant D10N) From Rhodobacter Sphaeroides in Complex with Xylulose-(1,5)Bisphosphate, Crystal Form II within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:13.8 occ:1.00 O2P A:XBP301 1.9 12.2 1.0 OD2 A:ASP8 2.0 15.2 1.0 OD1 A:ASP176 2.1 15.1 1.0 O A:HOH510 2.1 15.3 1.0 O A:HOH511 2.2 15.7 1.0 O A:ASN10 2.2 15.2 1.0 CG A:ASP8 2.9 14.5 1.0 CG A:ASP176 3.1 14.2 1.0 OD1 A:ASP8 3.2 14.1 1.0 C A:ASN10 3.4 15.1 1.0 P1 A:XBP301 3.4 14.5 1.0 OD2 A:ASP176 3.4 16.2 1.0 OE1 A:GLU175 4.0 13.8 1.0 N A:ASN10 4.0 14.2 1.0 O A:HOH520 4.0 16.6 1.0 O3P A:XBP301 4.0 15.3 1.0 CA A:ASN10 4.1 14.7 1.0 OG1 A:THR12 4.1 15.5 1.0 O1P A:XBP301 4.2 16.7 1.0 CB A:ASP8 4.2 14.6 1.0 OG A:SER177 4.3 14.9 1.0 CB A:ASN10 4.3 14.5 1.0 O1 A:XBP301 4.4 14.7 1.0 CB A:ASP176 4.4 14.2 1.0 N A:GLY11 4.4 14.8 1.0 O A:HOH521 4.5 18.6 1.0 C1 A:XBP301 4.6 14.7 1.0 CA A:GLY11 4.7 14.9 1.0 N A:ASP176 4.7 13.1 1.0 C A:VAL9 4.7 14.7 1.0 CB A:SER177 4.7 13.8 1.0 O A:HOH548 4.8 27.1 1.0 O A:HOH535 4.8 20.3 1.0 N A:THR12 4.9 15.1 1.0 N A:VAL9 4.9 13.4 1.0 N A:SER177 4.9 14.2 1.0 C A:GLY11 5.0 15.0 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Cbby (Mutant D10N) From Rhodobacter Sphaeroides in Complex with Xylulose-(1,5)Bisphosphate, Crystal Form II


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 Cbby (Mutant D10N) From Rhodobacter Sphaeroides in Complex with Xylulose-(1,5)Bisphosphate, Crystal Form II within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg302 b:13.8 occ:1.00 O2P B:XBP301 2.0 13.3 1.0 OD2 B:ASP8 2.0 15.8 1.0 OD1 B:ASP176 2.0 15.1 1.0 O B:HOH496 2.1 14.3 1.0 O B:HOH497 2.1 15.5 1.0 O B:ASN10 2.2 14.6 1.0 CG B:ASP8 2.9 14.2 1.0 CG B:ASP176 3.1 14.6 1.0 OD1 B:ASP8 3.1 14.5 1.0 C B:ASN10 3.4 14.4 1.0 P1 B:XBP301 3.4 14.8 1.0 OD2 B:ASP176 3.5 16.5 1.0 O3P B:XBP301 4.0 16.6 1.0 O B:HOH503 4.0 15.6 1.0 N B:ASN10 4.0 13.7 1.0 OE1 B:GLU175 4.0 13.8 1.0 CA B:ASN10 4.1 13.6 1.0 O1P B:XBP301 4.2 17.7 1.0 OG1 B:THR12 4.2 14.9 1.0 CB B:ASP8 4.2 13.8 1.0 CB B:ASN10 4.3 13.9 1.0 OG B:SER177 4.3 15.9 1.0 CB B:ASP176 4.4 14.0 1.0 O1 B:XBP301 4.4 16.2 1.0 N B:GLY11 4.4 14.8 1.0 O B:HOH532 4.5 22.0 1.0 C1 B:XBP301 4.6 17.0 1.0 N B:ASP176 4.7 13.0 1.0 CB B:SER177 4.7 14.3 1.0 CA B:GLY11 4.7 13.7 1.0 C B:VAL9 4.7 13.4 1.0 O B:HOH570 4.8 27.4 1.0 O B:HOH542 4.8 23.8 1.0 N B:VAL9 4.9 12.9 1.0 N B:THR12 4.9 13.8 1.0 N B:SER177 5.0 13.7 1.0

A.Bracher, A.Sharma, A.Starling-Windhof, F.U.Hartl, M.Hayer-Hartl. Degradation of Potent Rubisco Inhibitor By Selective Sugar Phosphatase Nat.Plants 2015.
DOI: 10.1038/NPLANTS.2014.2