Magnesium in PDB 6ax9: F95N Epi-Isozizaene Synthase

All present enzymatic activity of F95N Epi-Isozizaene Synthase:
4.2.3.37;

The structure of F95N Epi-Isozizaene Synthase, PDB code: 6ax9 was solved by P.N.Blank, G.H.Barrow, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.95 / 2.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.851, 47.180, 75.490, 90.00, 95.95, 90.00
R / Rfree (%)	18.6 / 24.3

The binding sites of Magnesium atom in the F95N Epi-Isozizaene Synthase (pdb code 6ax9). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the F95N Epi-Isozizaene Synthase, PDB code: 6ax9:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the F95N Epi-Isozizaene Synthase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of F95N Epi-Isozizaene Synthase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:25.8 occ:1.00 O A:HOH504 2.1 24.3 1.0 O3 A:POP404 2.1 22.6 1.0 OD1 A:ASP99 2.2 31.6 1.0 O A:HOH514 2.2 30.8 1.0 O A:HOH525 2.3 31.7 1.0 O A:HOH501 2.4 31.2 1.0 P1 A:POP404 3.2 32.9 1.0 O2 A:POP404 3.2 21.1 1.0 CG A:ASP99 3.3 30.5 1.0 MG A:MG402 3.3 33.0 1.0 OD2 A:ASP99 3.6 31.8 1.0 OH A:TYR172 3.9 34.1 1.0 OE1 A:GLU175 4.0 32.2 1.0 O1 A:POP404 4.0 33.6 1.0 CZ A:TYR172 4.2 27.9 1.0 OE2 A:GLU175 4.2 36.0 1.0 O A:HOH507 4.3 31.8 1.0 O A:HOH512 4.4 34.8 1.0 O A:POP404 4.4 30.6 1.0 CE2 A:TYR172 4.5 29.8 1.0 CD A:GLU175 4.5 31.8 1.0 CB A:ASP99 4.6 30.5 1.0 NH1 A:ARG194 4.6 30.9 1.0 O6 A:POP404 4.7 32.3 1.0 O A:HOH506 4.7 34.4 1.0 O A:THR197 4.7 23.9 1.0 CE1 A:TYR172 4.9 26.9 1.0

Magnesium binding site 2 out of 3 in the F95N Epi-Isozizaene Synthase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of F95N Epi-Isozizaene Synthase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:33.0 occ:1.00 OD2 A:ASP99 2.0 31.8 1.0 O3 A:POP404 2.1 22.6 1.0 O6 A:POP404 2.1 32.3 1.0 O A:HOH507 2.1 31.8 1.0 O A:HOH514 2.1 30.8 1.0 O A:HOH524 2.2 28.2 1.0 CG A:ASP99 2.9 30.5 1.0 OD1 A:ASP99 3.2 31.6 1.0 MG A:MG401 3.3 25.8 1.0 P1 A:POP404 3.4 32.9 1.0 P2 A:POP404 3.4 24.9 1.0 O A:POP404 3.7 30.6 1.0 O A:HOH509 3.8 30.9 1.0 NH2 A:ARG338 4.0 27.6 1.0 NZ A:LYS247 4.0 33.8 1.0 O A:HOH512 4.0 34.8 1.0 O1 A:POP404 4.1 33.6 1.0 O A:HOH525 4.2 31.7 1.0 O4 A:POP404 4.2 31.0 1.0 CB A:ASP99 4.3 30.5 1.0 OE2 A:GLU248 4.3 33.4 1.0 O5 A:POP404 4.5 30.8 1.0 O2 A:POP404 4.5 21.1 1.0 OE1 A:GLU253 4.7 39.2 1.0 MG A:MG403 4.7 27.4 1.0 O A:HOH504 4.9 24.3 1.0 CE A:LYS247 4.9 36.5 1.0 O A:ASP99 4.9 34.2 1.0

Magnesium binding site 3 out of 3 in the F95N Epi-Isozizaene Synthase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of F95N Epi-Isozizaene Synthase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:27.4 occ:1.00 OD1 A:ASN240 1.9 27.9 1.0 O1 A:POP404 2.0 33.6 1.0 OE2 A:GLU248 2.1 33.4 1.0 O4 A:POP404 2.1 31.0 1.0 O A:HOH513 2.2 30.6 1.0 OG A:SER244 2.5 22.3 1.0 CG A:ASN240 2.8 27.1 1.0 O A:POP404 2.9 30.6 1.0 P1 A:POP404 3.0 32.9 1.0 P2 A:POP404 3.0 24.9 1.0 ND2 A:ASN240 3.1 31.5 1.0 CD A:GLU248 3.2 33.6 1.0 CB A:SER244 3.3 26.3 1.0 O A:HOH507 3.7 31.8 1.0 OE1 A:GLU248 3.7 30.5 1.0 NH2 A:ARG194 3.7 26.4 1.0 O6 A:POP404 3.7 32.3 1.0 O3 A:POP404 3.9 22.6 1.0 O2 A:POP404 4.1 21.1 1.0 O5 A:POP404 4.2 30.8 1.0 CB A:ASN240 4.3 28.2 1.0 CG A:GLU248 4.4 33.4 1.0 O A:ASN240 4.4 27.0 1.0 OD1 A:ASP241 4.5 29.0 1.0 C A:ASN240 4.5 24.7 1.0 NZ A:LYS247 4.5 33.8 1.0 MG A:MG402 4.7 33.0 1.0 CA A:SER244 4.7 30.5 1.0 CZ A:ARG194 4.7 31.4 1.0 N A:ASP241 4.8 24.8 1.0 CA A:ASP241 4.9 26.6 1.0

P.N.Blank, G.H.Barrow, W.K.W.Chou, L.Duan, D.E.Cane, D.W.Christianson. Substitution of Aromatic Residues with Polar Residues in the Active Site Pocket of Epi-Isozizaene Synthase Leads to the Generation of New Cyclic Sesquiterpenes. Biochemistry V. 56 5798 2017.
ISSN: ISSN 1520-4995
PubMed: 28967743
DOI: 10.1021/ACS.BIOCHEM.7B00895