Magnesium in PDB 6ggk: Crystal Structure of COTB2 C-Terminal Truncation

All present enzymatic activity of Crystal Structure of COTB2 C-Terminal Truncation:
4.2.3.146;

The structure of Crystal Structure of COTB2 C-Terminal Truncation, PDB code: 6ggk was solved by R.Driller, S.Janke, M.Fuchs, E.Warner, A.R.Mhashal, D.T.Major, M.Christmann, T.Brueck, B.Loll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.86 / 2.15
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	61.010, 99.714, 107.718, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / 24.1

The structure of Crystal Structure of COTB2 C-Terminal Truncation also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of COTB2 C-Terminal Truncation (pdb code 6ggk). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of COTB2 C-Terminal Truncation, PDB code: 6ggk:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Crystal Structure of COTB2 C-Terminal Truncation


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 COTB2 C-Terminal Truncation within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:39.4 occ:1.00 O A:HOH483 2.1 33.0 1.0 OE1 A:GLU228 2.2 37.4 1.0 O A:HOH423 2.2 29.2 1.0 O A:HOH479 2.3 37.9 1.0 OD1 A:ASN220 2.3 31.4 1.0 OG A:SER224 2.4 35.5 1.0 CD A:GLU228 3.2 37.4 1.0 CG A:ASN220 3.3 26.5 1.0 CB A:SER224 3.3 30.9 1.0 ND2 A:ASN220 3.6 27.5 1.0 OE2 A:GLU228 3.7 33.6 1.0 O A:ASN220 4.0 27.3 1.0 NH2 A:ARG177 4.3 28.6 1.0 CG A:GLU228 4.4 31.6 1.0 C A:ASN220 4.5 25.2 1.0 OD1 A:ASP221 4.6 27.4 1.0 CB A:ASN220 4.7 25.4 1.0 CA A:SER224 4.7 28.0 1.0

Magnesium binding site 2 out of 3 in the Crystal Structure of COTB2 C-Terminal Truncation


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 COTB2 C-Terminal Truncation within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:36.2 occ:1.00 O B:HOH440 1.9 40.5 1.0 O B:HOH406 2.1 29.7 1.0 OD1 B:ASN220 2.2 32.7 1.0 O B:HOH476 2.3 40.8 1.0 OE2 B:GLU228 2.3 42.8 1.0 OG B:SER224 2.3 31.8 1.0 CD B:GLU228 3.1 37.1 1.0 CB B:SER224 3.3 31.8 1.0 OE1 B:GLU228 3.3 33.9 1.0 CG B:ASN220 3.4 28.9 1.0 O B:ASN220 3.9 30.1 1.0 ND2 B:ASN220 4.0 36.4 1.0 NH2 B:ARG177 4.1 26.3 1.0 OD1 B:ASP221 4.3 26.0 1.0 C B:ASN220 4.3 28.6 1.0 CG B:GLU228 4.4 33.9 1.0 CB B:ASN220 4.6 22.8 1.0 CA B:SER224 4.6 25.7 1.0 CA B:ASP221 4.7 23.4 1.0 N B:ASP221 4.7 21.0 1.0

Magnesium binding site 3 out of 3 in the Crystal Structure of COTB2 C-Terminal Truncation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of COTB2 C-Terminal Truncation within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg302 b:49.1 occ:0.80 O B:HOH438 1.9 47.7 0.8 O B:HOH417 2.0 39.6 0.8 O B:HOH455 2.1 43.9 0.8 OD1 B:ASP110 2.4 48.1 1.0 OD1 B:ASP153 3.2 48.0 1.0 CG B:ASP110 3.3 51.7 1.0 OD2 B:ASP110 3.5 51.2 1.0 OD1 B:ASP180 4.0 31.2 1.0 CG B:ASP153 4.1 45.0 1.0 O B:ASP180 4.2 27.6 1.0 OD2 B:ASP180 4.5 35.1 1.0 CG B:ASP180 4.7 27.7 1.0 CB B:ASP110 4.7 49.1 1.0 OD2 B:ASP153 4.8 47.6 1.0 CZ B:PHE149 4.9 31.2 1.0 NH2 B:ARG157 4.9 52.6 1.0 CB B:ASP153 4.9 33.6 1.0

R.Driller, S.Janke, M.Fuchs, E.Warner, A.R.Mhashal, D.T.Major, M.Christmann, T.Bruck, B.Loll. Towards A Comprehensive Understanding of the Structural Dynamics of A Bacterial Diterpene Synthase During Catalysis. Nat Commun V. 9 3971 2018.
ISSN: ESSN 2041-1723
PubMed: 30266969
DOI: 10.1038/S41467-018-06325-8