Magnesium in PDB 7ao5: Crystal Structure of COTB2 Variant W288F

All present enzymatic activity of Crystal Structure of COTB2 Variant W288F:
4.2.3.146;

The structure of Crystal Structure of COTB2 Variant W288F, PDB code: 7ao5 was solved by N.Dimos, R.Driller, B.Loll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.49 / 2.06
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	101.117, 107.575, 61.899, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 23.9

The binding sites of Magnesium atom in the Crystal Structure of COTB2 Variant W288F (pdb code 7ao5). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of COTB2 Variant W288F, PDB code: 7ao5:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Crystal Structure of COTB2 Variant W288F


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 Variant W288F within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:53.6 occ:1.00 O A:HOH506 2.1 27.6 1.0 O A:HOH640 2.2 50.5 1.0 OE2 A:GLU228 2.3 47.7 1.0 O A:HOH644 2.3 35.6 1.0 OD1 A:ASN220 2.4 52.0 1.0 OG A:SER224 2.7 38.3 1.0 CD A:GLU228 3.1 29.0 1.0 OE1 A:GLU228 3.3 41.0 1.0 O A:HOH625 3.5 37.5 1.0 CG A:ASN220 3.6 44.2 1.0 CB A:SER224 3.7 33.1 1.0 NH2 A:ARG177 3.8 26.8 1.0 OD1 A:ASP221 4.2 26.6 1.0 O A:ASN220 4.2 27.2 1.0 ND2 A:ASN220 4.2 49.5 1.0 CG A:GLU228 4.4 30.1 1.0 C A:ASN220 4.5 27.4 1.0 CB A:ASN220 4.7 27.4 1.0 O A:THR235 4.8 34.2 1.0 CA A:ASP221 4.8 23.4 1.0 NH2 A:ARG227 4.8 65.5 1.0 N A:ASP221 4.8 17.2 1.0

Magnesium binding site 2 out of 4 in the Crystal Structure of COTB2 Variant W288F


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 Variant W288F within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg404 b:50.5 occ:1.00 O A:HOH543 2.2 38.4 1.0 O A:HOH560 2.2 34.3 1.0 O A:HOH567 2.4 46.4 1.0 O A:HOH534 2.6 36.4 1.0 OD1 A:ASP110 2.9 61.3 1.0 OD2 A:ASP110 3.2 72.3 1.0 CG A:ASP110 3.4 61.0 1.0 OD1 A:ASP153 4.0 55.1 1.0 O A:ASP180 4.5 29.0 1.0 OD1 A:ASP180 4.5 28.5 1.0 OD2 A:ASP180 4.7 30.4 1.0 CG A:ASP153 4.8 50.1 1.0 CB A:ASP110 4.9 47.7 1.0 O A:HOH625 4.9 37.5 1.0 CG A:ASP180 4.9 30.1 1.0

Magnesium binding site 3 out of 4 in the Crystal Structure of COTB2 Variant W288F


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 Variant W288F within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg402 b:45.6 occ:1.00 O B:HOH526 2.0 33.5 1.0 O B:HOH612 2.1 35.5 1.0 OE2 B:GLU228 2.1 38.3 1.0 OD1 B:ASN220 2.4 40.3 1.0 OG B:SER224 2.5 35.7 1.0 O B:HOH633 2.5 34.0 1.0 CD B:GLU228 3.1 34.5 1.0 CB B:SER224 3.4 31.2 1.0 OE1 B:GLU228 3.4 28.0 1.0 CG B:ASN220 3.5 40.1 1.0 O B:HOH553 3.7 36.1 1.0 O B:ASN220 4.0 25.8 1.0 NH2 B:ARG177 4.1 24.5 1.0 ND2 B:ASN220 4.2 43.5 1.0 O B:HOH599 4.2 52.3 1.0 OD1 B:ASP221 4.4 24.4 1.0 CG B:GLU228 4.4 37.4 1.0 C B:ASN220 4.4 25.5 1.0 CB B:ASN220 4.8 28.7 1.0 CA B:SER224 4.8 27.8 1.0 O B:THR235 4.8 34.0 1.0 CA B:ASP221 4.8 23.5 1.0 N B:ASP221 4.9 21.8 1.0

Magnesium binding site 4 out of 4 in the Crystal Structure of COTB2 Variant W288F


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of COTB2 Variant W288F within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg403 b:61.6 occ:1.00 O B:HOH605 2.2 49.6 1.0 O B:HOH651 2.2 54.4 1.0 O B:HOH524 2.3 43.2 1.0 OD1 B:ASP110 3.1 75.6 1.0 OD2 B:ASP110 3.5 67.7 1.0 CG B:ASP110 3.7 67.9 1.0 O B:HOH633 4.1 34.0 1.0 OD2 B:ASP180 4.4 22.4 1.0 O B:HOH553 4.4 36.1 1.0 OD1 B:ASP153 4.5 54.7 1.0 O B:ASP180 4.5 28.7 1.0 NH1 B:ARG177 4.7 26.9 1.0 OD1 B:ASP180 4.8 33.1 1.0 CG B:ASP180 5.0 21.5 1.0

K.Raz, R.Driller, N.Dimos, M.Ringel, T.Brueck, B.Loll, D.T.Major. A Delusion of A Non-Existing Catalytic Effect: the Role of COTB2 in Guiding the Complex Biosynthesis of Cyclooctat-9-En-Ol To Be Published.