Magnesium in PDB 7qt1: Non-Obligately L8S8-Complex Forming Rubisco Derived From Ancestral Sequence Reconstruction and Rational Engineering in L8S8 Complex with Substitution E170N

The structure of Non-Obligately L8S8-Complex Forming Rubisco Derived From Ancestral Sequence Reconstruction and Rational Engineering in L8S8 Complex with Substitution E170N, PDB code: 7qt1 was solved by J.Zarzycki, L.Schulz, T.J.Erb, G.K.A.Hochberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.29 / 2.10
Space group	I 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	108.942, 106.604, 191.968, 90, 98.78, 90
R / Rfree (%)	16.3 / 18.6

The binding sites of Magnesium atom in the Non-Obligately L8S8-Complex Forming Rubisco Derived From Ancestral Sequence Reconstruction and Rational Engineering in L8S8 Complex with Substitution E170N (pdb code 7qt1). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Non-Obligately L8S8-Complex Forming Rubisco Derived From Ancestral Sequence Reconstruction and Rational Engineering in L8S8 Complex with Substitution E170N, PDB code: 7qt1:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Non-Obligately L8S8-Complex Forming Rubisco Derived From Ancestral Sequence Reconstruction and Rational Engineering in L8S8 Complex with Substitution E170N


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Non-Obligately L8S8-Complex Forming Rubisco Derived From Ancestral Sequence Reconstruction and Rational Engineering in L8S8 Complex with Substitution E170N within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:10.3 occ:1.00 OQ2 A:KCX187 2.1 10.2 1.0 OE1 A:GLU190 2.1 10.2 1.0 OD1 A:ASP189 2.1 10.2 1.0 O7 A:CAP501 2.1 10.4 1.0 O3 A:CAP501 2.1 10.6 1.0 O2 A:CAP501 2.3 10.4 1.0 C2 A:CAP501 2.8 10.5 1.0 C A:CAP501 2.8 10.4 1.0 CX A:KCX187 3.0 10.3 1.0 C3 A:CAP501 3.0 10.4 1.0 CD A:GLU190 3.1 10.3 1.0 OQ1 A:KCX187 3.2 11.0 1.0 CG A:ASP189 3.2 10.4 1.0 OE2 A:GLU190 3.6 10.8 1.0 N A:GLU190 3.8 10.1 1.0 NZ A:LYS163 3.9 10.3 1.0 CG2 A:THR159 4.0 10.4 1.0 NZ A:LYS161 4.0 10.4 1.0 CA A:ASP189 4.0 10.1 1.0 NE2 A:HIS280 4.0 10.2 1.0 O6 A:CAP501 4.1 10.5 1.0 OD2 A:ASP189 4.1 12.5 1.0 CB A:ASP189 4.1 10.2 1.0 NZ A:KCX187 4.2 10.2 1.0 C4 A:CAP501 4.2 10.5 1.0 OG1 A:THR159 4.3 10.5 1.0 C1 A:CAP501 4.3 10.6 1.0 CG A:GLU190 4.4 10.1 1.0 C A:ASP189 4.5 10.1 1.0 CB A:GLU190 4.5 10.1 1.0 CB A:THR159 4.7 10.5 1.0 CD2 A:HIS280 4.7 10.2 1.0 C5 A:CAP501 4.7 10.4 1.0 O1 A:CAP501 4.8 10.6 1.0 CA A:GLU190 4.8 10.0 1.0 CE1 A:HIS280 5.0 10.2 1.0

Magnesium binding site 2 out of 4 in the Non-Obligately L8S8-Complex Forming Rubisco Derived From Ancestral Sequence Reconstruction and Rational Engineering in L8S8 Complex with Substitution E170N


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Non-Obligately L8S8-Complex Forming Rubisco Derived From Ancestral Sequence Reconstruction and Rational Engineering in L8S8 Complex with Substitution E170N within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg502 b:11.9 occ:1.00 OD1 C:ASP189 2.0 11.2 1.0 OE1 C:GLU190 2.0 11.4 1.0 O6 C:CAP501 2.1 11.1 1.0 O3 C:CAP501 2.2 10.9 1.0 OQ2 C:KCX187 2.2 13.7 1.0 O2 C:CAP501 2.3 11.7 1.0 C C:CAP501 2.9 11.1 1.0 C2 C:CAP501 2.9 11.1 1.0 CD C:GLU190 3.1 12.2 1.0 C3 C:CAP501 3.1 11.0 1.0 CG C:ASP189 3.2 11.7 1.0 CX C:KCX187 3.2 11.2 1.0 OQ1 C:KCX187 3.4 10.8 1.0 OE2 C:GLU190 3.5 10.9 1.0 NZ C:LYS163 3.7 11.1 1.0 N C:GLU190 3.8 10.7 1.0 NZ C:LYS161 3.9 11.2 1.0 OD2 C:ASP189 4.0 11.9 1.0 CA C:ASP189 4.0 11.1 1.0 CG2 C:THR159 4.0 11.0 1.0 NE2 C:HIS280 4.1 10.7 1.0 CB C:ASP189 4.1 10.9 1.0 O7 C:CAP501 4.1 12.0 1.0 OG1 C:THR159 4.3 11.0 1.0 C4 C:CAP501 4.3 11.0 1.0 CG C:GLU190 4.4 10.7 1.0 NZ C:KCX187 4.4 11.6 1.0 C1 C:CAP501 4.4 11.2 1.0 C C:ASP189 4.4 10.7 1.0 CB C:GLU190 4.6 10.6 1.0 CD2 C:HIS280 4.7 10.6 1.0 CB C:THR159 4.7 11.5 1.0 O1 C:CAP501 4.8 11.2 1.0 CA C:GLU190 4.8 10.6 1.0 C5 C:CAP501 4.8 12.8 1.0 CE1 C:HIS280 5.0 10.6 1.0

Magnesium binding site 3 out of 4 in the Non-Obligately L8S8-Complex Forming Rubisco Derived From Ancestral Sequence Reconstruction and Rational Engineering in L8S8 Complex with Substitution E170N


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Non-Obligately L8S8-Complex Forming Rubisco Derived From Ancestral Sequence Reconstruction and Rational Engineering in L8S8 Complex with Substitution E170N within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg502 b:10.9 occ:1.00 OE1 E:GLU190 2.0 12.0 1.0 OD1 E:ASP189 2.0 10.9 1.0 O6 E:CAP501 2.1 11.6 1.0 OQ1 E:KCX187 2.1 10.8 1.0 O3 E:CAP501 2.1 10.9 1.0 O2 E:CAP501 2.3 11.6 1.0 C E:CAP501 2.8 11.1 1.0 C2 E:CAP501 2.8 11.1 1.0 C3 E:CAP501 3.0 11.1 1.0 CD E:GLU190 3.1 10.7 1.0 CX E:KCX187 3.1 10.9 1.0 CG E:ASP189 3.2 11.5 1.0 OQ2 E:KCX187 3.4 12.9 1.0 OE2 E:GLU190 3.5 10.7 1.0 NZ E:LYS163 3.7 10.8 1.0 N E:GLU190 3.7 10.6 1.0 NZ E:LYS161 3.9 11.1 1.0 OD2 E:ASP189 4.0 13.1 1.0 CG2 E:THR159 4.0 10.9 1.0 O7 E:CAP501 4.0 11.2 1.0 CA E:ASP189 4.0 10.6 1.0 NE2 E:HIS280 4.1 10.8 1.0 CB E:ASP189 4.1 10.7 1.0 C4 E:CAP501 4.2 11.1 1.0 OG1 E:THR159 4.3 11.1 1.0 NZ E:KCX187 4.3 10.8 1.0 CG E:GLU190 4.3 10.6 1.0 C1 E:CAP501 4.3 11.2 1.0 C E:ASP189 4.4 10.6 1.0 CB E:GLU190 4.5 10.5 1.0 CD2 E:HIS280 4.7 10.7 1.0 CB E:THR159 4.7 11.1 1.0 C5 E:CAP501 4.7 11.1 1.0 CA E:GLU190 4.7 10.5 1.0 O1 E:CAP501 4.8 11.3 1.0 O E:HOH774 4.9 12.2 1.0 CE1 E:HIS280 5.0 10.7 1.0

Magnesium binding site 4 out of 4 in the Non-Obligately L8S8-Complex Forming Rubisco Derived From Ancestral Sequence Reconstruction and Rational Engineering in L8S8 Complex with Substitution E170N


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Non-Obligately L8S8-Complex Forming Rubisco Derived From Ancestral Sequence Reconstruction and Rational Engineering in L8S8 Complex with Substitution E170N within 5.0Å range: probe atom residue distance (Å) B Occ G:Mg502 b:12.1 occ:1.00 OE1 G:GLU190 1.9 10.7 1.0 OD1 G:ASP189 2.0 12.5 1.0 O7 G:CAP501 2.1 10.9 1.0 O3 G:CAP501 2.2 11.3 1.0 OQ1 G:KCX187 2.2 13.0 1.0 O2 G:CAP501 2.3 13.1 1.0 C G:CAP501 2.9 12.0 1.0 C2 G:CAP501 2.9 12.3 1.0 CD G:GLU190 3.0 11.6 1.0 C3 G:CAP501 3.0 11.9 1.0 CX G:KCX187 3.2 12.3 1.0 CG G:ASP189 3.2 13.0 1.0 OE2 G:GLU190 3.4 12.3 1.0 OQ2 G:KCX187 3.5 12.2 1.0 NZ G:LYS163 3.7 10.9 1.0 N G:GLU190 3.8 11.5 1.0 NZ G:LYS161 4.0 11.1 1.0 CA G:ASP189 4.0 10.6 1.0 NE2 G:HIS280 4.0 11.5 1.0 OD2 G:ASP189 4.0 14.5 1.0 CB G:ASP189 4.1 11.0 1.0 O6 G:CAP501 4.1 11.7 1.0 CG2 G:THR159 4.1 11.5 1.0 C4 G:CAP501 4.3 10.9 1.0 CG G:GLU190 4.3 10.5 1.0 C1 G:CAP501 4.4 11.1 1.0 OG1 G:THR159 4.4 12.6 1.0 NZ G:KCX187 4.4 10.6 1.0 C G:ASP189 4.4 10.8 1.0 CB G:GLU190 4.5 10.5 1.0 CD2 G:HIS280 4.6 10.7 1.0 C5 G:CAP501 4.8 11.9 1.0 O1 G:CAP501 4.8 11.4 1.0 CA G:GLU190 4.8 10.4 1.0 CB G:THR159 4.8 11.7 1.0 CE1 G:HIS280 4.9 10.5 1.0

L.Schulz, Z.Guo, J.Zarzycki, W.Steinchen, J.M.Schuller, T.Heimerl, S.Prinz, O.Mueller-Cajar, T.J.Erb, G.K.A.Hochberg. Evolution of Increased Complexity and Specificity at the Dawn of Form I Rubiscos. Science V. 378 155 2022.
ISSN: ESSN 1095-9203
PubMed: 36227987
DOI: 10.1126/SCIENCE.ABQ1416