Magnesium in PDB 9rub: Crystal Structure of Activated Ribulose-1,5-Bisphosphate Carboxylase Complexed with Its Substrate, Ribulose-1,5-Bisphosphate

All present enzymatic activity of Crystal Structure of Activated Ribulose-1,5-Bisphosphate Carboxylase Complexed with Its Substrate, Ribulose-1,5-Bisphosphate:
4.1.1.39;

The structure of Crystal Structure of Activated Ribulose-1,5-Bisphosphate Carboxylase Complexed with Its Substrate, Ribulose-1,5-Bisphosphate, PDB code: 9rub was solved by T.Lundqvist, G.Schneider, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 2.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	65.500, 70.600, 104.100, 90.00, 92.10, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Magnesium atom in the Crystal Structure of Activated Ribulose-1,5-Bisphosphate Carboxylase Complexed with Its Substrate, Ribulose-1,5-Bisphosphate (pdb code 9rub). 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 Activated Ribulose-1,5-Bisphosphate Carboxylase Complexed with Its Substrate, Ribulose-1,5-Bisphosphate, PDB code: 9rub:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Activated Ribulose-1,5-Bisphosphate Carboxylase Complexed with Its Substrate, Ribulose-1,5-Bisphosphate


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 Activated Ribulose-1,5-Bisphosphate Carboxylase Complexed with Its Substrate, Ribulose-1,5-Bisphosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg500 b:21.1 occ:1.00 O1 A:FMT601 2.4 20.1 1.0 O2 A:FMT601 2.4 19.7 1.0 O2 A:RUB600 2.5 20.6 1.0 OD1 A:ASP193 2.5 17.3 1.0 O3 A:RUB600 2.6 21.0 1.0 C A:FMT601 2.8 17.0 1.0 C3 A:RUB600 3.0 20.9 1.0 C2 A:RUB600 3.1 21.1 1.0 C4 A:RUB600 3.2 20.8 1.0 CG A:ASP193 3.4 16.8 1.0 O4 A:RUB600 3.5 20.3 1.0 OD2 A:ASP193 3.7 17.0 1.0 OE2 A:GLU194 3.7 24.2 1.0 CD A:GLU194 4.1 23.1 1.0 CE1 A:HIS287 4.2 19.1 1.0 CD1 A:ILE164 4.2 14.7 1.0 NZ A:LYS191 4.3 16.1 1.0 OE1 A:GLU194 4.4 23.1 1.0 CG1 A:ILE164 4.5 15.1 1.0 C1 A:RUB600 4.6 22.2 1.0 CB A:ASP193 4.6 16.0 1.0 NE2 A:HIS287 4.7 19.0 1.0 CG2 A:ILE164 4.7 15.1 1.0 C5 A:RUB600 4.7 21.4 1.0 N A:GLU194 4.8 18.8 1.0 ND1 A:HIS287 4.8 18.8 1.0 CA A:ASP193 4.8 15.5 1.0 CE A:LYS191 4.8 13.6 1.0 ND2 B:ASN111 5.0 38.8 1.0 O1 A:RUB600 5.0 23.5 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Activated Ribulose-1,5-Bisphosphate Carboxylase Complexed with Its Substrate, Ribulose-1,5-Bisphosphate


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 Activated Ribulose-1,5-Bisphosphate Carboxylase Complexed with Its Substrate, Ribulose-1,5-Bisphosphate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg500 b:16.6 occ:1.00 O3 B:RUB700 2.2 22.5 1.0 O2 B:RUB700 2.4 21.5 1.0 O1 B:FMT701 2.5 17.0 1.0 OD1 B:ASP193 2.5 17.7 1.0 C2 B:RUB700 2.9 22.0 1.0 C3 B:RUB700 3.0 22.3 1.0 O2 B:FMT701 3.2 18.5 1.0 CG B:ASP193 3.3 16.9 1.0 C B:FMT701 3.3 14.5 1.0 OE1 B:GLU194 3.5 12.4 1.0 OD2 B:ASP193 3.6 18.2 1.0 CD B:GLU194 3.6 11.3 1.0 CG B:GLU194 3.8 9.9 1.0 OE2 B:GLU194 4.1 12.4 1.0 C4 B:RUB700 4.1 22.0 1.0 C1 B:RUB700 4.1 22.7 1.0 O4 B:RUB700 4.5 21.0 1.0 CB B:ASP193 4.5 14.8 1.0 CE B:LYS168 4.6 28.4 1.0 ND2 A:ASN111 4.7 42.4 1.0 CG1 B:ILE164 4.7 13.5 1.0 CE1 B:HIS287 4.7 14.5 1.0 CA B:ASP193 4.7 12.6 1.0 NZ B:LYS191 4.8 15.6 1.0 CD1 B:ILE164 4.8 12.9 1.0 CG2 B:ILE164 4.8 14.2 1.0 N B:GLU194 4.9 9.9 1.0

T.Lundqvist, G.Schneider. Crystal Structure of Activated Ribulose-1,5-Bisphosphate Carboxylase Complexed with Its Substrate, Ribulose-1,5-Bisphosphate. J.Biol.Chem. V. 266 12604 1991.
ISSN: ISSN 0021-9258
PubMed: 1905726