Manganese in PDB 6aob: Crystal Structure of Non-Canonical Dimeric Guanylyl Cyclase Domain of Rhogc Fusion Protein From the Aquatic Fungus Blastocladiella Emersonii

The structure of Crystal Structure of Non-Canonical Dimeric Guanylyl Cyclase Domain of Rhogc Fusion Protein From the Aquatic Fungus Blastocladiella Emersonii, PDB code: 6aob was solved by R.Prem Kumar, D.D.Oprian, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.97 / 1.70
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	91.769, 95.880, 100.049, 90.00, 90.00, 90.00
R / Rfree (%)	16.4 / 19.6

The binding sites of Manganese atom in the Crystal Structure of Non-Canonical Dimeric Guanylyl Cyclase Domain of Rhogc Fusion Protein From the Aquatic Fungus Blastocladiella Emersonii (pdb code 6aob). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Non-Canonical Dimeric Guanylyl Cyclase Domain of Rhogc Fusion Protein From the Aquatic Fungus Blastocladiella Emersonii, PDB code: 6aob:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of Non-Canonical Dimeric Guanylyl Cyclase Domain of Rhogc Fusion Protein From the Aquatic Fungus Blastocladiella Emersonii


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Non-Canonical Dimeric Guanylyl Cyclase Domain of Rhogc Fusion Protein From the Aquatic Fungus Blastocladiella Emersonii within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn701 b:29.1 occ:1.00 O A:HOH819 2.0 24.4 1.0 O41 A:TLA702 2.1 21.8 1.0 OD2 B:ASP457 2.1 30.5 1.0 OD1 A:ASP501 2.3 24.0 1.0 O B:HOH892 2.3 29.0 1.0 O3 A:TLA702 2.4 27.1 1.0 C4 A:TLA702 3.0 24.0 1.0 CG A:ASP501 3.2 24.8 1.0 C3 A:TLA702 3.3 22.8 1.0 CG B:ASP457 3.4 26.6 1.0 OD2 A:ASP501 3.5 27.5 1.0 O A:HOH917 3.6 21.8 0.5 O2 A:TLA702 3.7 23.1 1.0 OD1 A:ASP457 3.8 34.6 1.0 O B:HOH832 3.9 28.2 1.0 O A:HOH917 4.0 18.6 0.6 NH1 B:ARG545 4.1 24.3 1.0 C2 A:TLA702 4.1 20.8 1.0 O4 A:TLA702 4.1 22.5 1.0 CB B:ASP457 4.1 19.2 1.0 MN B:MN701 4.2 25.8 1.0 O A:HOH801 4.2 19.7 1.0 OD1 B:ASP457 4.3 27.8 1.0 CB A:ASP501 4.6 20.8 1.0 OE2 B:GLU579 4.7 30.2 1.0 N A:ASP501 4.7 16.6 1.0 OE1 B:GLU579 4.8 35.9 1.0 C1 A:TLA702 4.9 21.6 1.0 CG A:ASP457 5.0 33.1 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of Non-Canonical Dimeric Guanylyl Cyclase Domain of Rhogc Fusion Protein From the Aquatic Fungus Blastocladiella Emersonii


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Non-Canonical Dimeric Guanylyl Cyclase Domain of Rhogc Fusion Protein From the Aquatic Fungus Blastocladiella Emersonii within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn701 b:25.8 occ:1.00 O A:HOH801 1.7 19.7 1.0 OD1 B:ASP501 2.0 23.0 1.0 O2 A:TLA702 2.1 23.1 1.0 OD2 B:ASP501 2.2 25.9 1.0 OD1 B:ASP457 2.3 27.8 1.0 O11 A:TLA702 2.3 20.5 1.0 CG B:ASP501 2.4 22.1 1.0 CG B:ASP457 2.9 26.6 1.0 OD2 B:ASP457 2.9 30.5 1.0 C1 A:TLA702 3.0 21.6 1.0 C2 A:TLA702 3.0 20.8 1.0 O3 A:TLA702 3.6 27.1 1.0 CB B:ASP501 3.9 19.0 1.0 C3 A:TLA702 3.9 22.8 1.0 O A:HOH858 3.9 35.7 1.0 O A:HOH819 4.2 24.4 1.0 MN A:MN701 4.2 29.1 1.0 O1 A:TLA702 4.2 23.8 1.0 NH2 A:ARG545 4.3 23.8 0.7 CB B:ASP457 4.3 19.2 1.0 O B:ILE458 4.3 20.0 1.0 O B:HOH815 4.4 31.1 1.0 N B:ILE458 4.4 18.7 1.0 OD1 A:ASP457 4.4 34.6 1.0 C B:ASP501 4.5 19.0 1.0 C4 A:TLA702 4.6 24.0 1.0 CA B:ASP501 4.6 21.5 1.0 O A:HOH860 4.6 28.1 1.0 CB B:PHE461 4.6 18.0 1.0 N B:ASP501 4.6 19.4 1.0 N B:ALA502 4.7 19.4 1.0 CG B:PHE461 4.8 20.9 1.0 O41 A:TLA702 4.9 21.8 1.0 CA B:ASP457 4.9 17.6 1.0 O B:ASP501 4.9 21.3 1.0 CD2 B:PHE461 5.0 23.5 1.0

R.P.Kumar, B.R.Morehouse, J.Fofana, M.M.Trieu, D.H.Zhou, M.O.Lorenz, D.D.Oprian. Structure and Monomer/Dimer Equilibrium For the Guanylyl Cyclase Domain of the Optogenetics Protein Rhogc. J. Biol. Chem. V. 292 21578 2017.
ISSN: ESSN 1083-351X
PubMed: 29118188
DOI: 10.1074/JBC.M117.812685