Manganese in PDB 7nf2: Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct

All present enzymatic activity of Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct:
4.1.1.102;

The structure of Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct, PDB code: 7nf2 was solved by A.Saaret, D.Leys, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	115.12 / 1.33
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	74.54, 74.54, 345.36, 90, 90, 120
R / Rfree (%)	16.2 / 18.1

The structure of Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct also contains other interesting chemical elements:

Potassium

(K)

4 atoms

The binding sites of Manganese atom in the Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct (pdb code 7nf2). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct, PDB code: 7nf2:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1208 b:14.7 occ:1.00 ND2 A:ASN178 2.1 7.8 1.0 OE2 A:GLU243 2.1 9.7 1.0 O A:HOH1374 2.1 10.2 1.0 O7 A:JRH1205 2.1 10.3 1.0 O A:HOH1443 2.2 12.2 1.0 ND1 A:HIS201 2.3 11.0 1.0 CG A:ASN178 3.1 10.2 1.0 CE1 A:HIS201 3.2 11.1 1.0 CD A:GLU243 3.2 9.4 1.0 P1 A:JRH1205 3.3 9.9 1.0 CG A:HIS201 3.4 10.1 1.0 OD1 A:ASN178 3.5 12.4 1.0 OE1 A:GLU243 3.6 10.3 1.0 O9 A:JRH1205 3.6 10.8 1.0 K A:K1207 3.7 13.4 1.0 CB A:HIS201 3.8 10.4 1.0 O8 A:JRH1205 4.2 10.9 1.0 CG1 A:ILE237 4.3 12.1 1.0 O A:ILE237 4.3 11.3 1.0 NE2 A:HIS201 4.4 11.3 1.0 CZ2 A:TRP176 4.4 13.0 1.0 O A:VAL241 4.4 13.2 1.0 O6 A:JRH1205 4.5 9.6 1.0 CB A:ASN178 4.5 10.7 1.0 CG A:GLU243 4.5 10.1 1.0 CD2 A:HIS201 4.5 11.1 1.0 O A:TRP179 4.7 9.4 1.0 O A:PRO238 4.7 13.7 1.0 NE1 A:TRP176 4.8 12.3 1.0 CE2 A:TRP176 5.0 12.1 1.0

Manganese binding site 2 out of 2 in the Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of T. Atroviride Fdc Variant Tafdcv in Complex with Prfmn Crotonic Acid Adduct within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn906 b:19.6 occ:1.00 O8 B:JRH903 2.1 13.7 1.0 ND2 B:ASN178 2.1 12.1 1.0 OE2 B:GLU243 2.1 16.1 1.0 O B:HOH1101 2.1 15.0 1.0 O B:HOH1062 2.2 14.3 1.0 ND1 B:HIS201 2.3 13.7 1.0 CG B:ASN178 3.1 14.4 1.0 CE1 B:HIS201 3.2 14.2 1.0 CD B:GLU243 3.2 15.6 1.0 P1 B:JRH903 3.3 14.2 1.0 CG B:HIS201 3.4 12.9 1.0 OD1 B:ASN178 3.5 18.5 1.0 OE1 B:GLU243 3.5 14.3 1.0 O7 B:JRH903 3.6 14.9 1.0 K B:K905 3.7 17.8 1.0 CB B:HIS201 3.8 13.3 1.0 O9 B:JRH903 4.2 13.7 1.0 CG1 B:ILE237 4.3 17.9 1.0 CZ2 B:TRP176 4.3 17.3 1.0 O B:ILE237 4.3 16.9 1.0 NE2 B:HIS201 4.4 14.7 1.0 O6 B:JRH903 4.4 14.0 1.0 CB B:ASN178 4.5 14.8 1.0 CD2 B:HIS201 4.5 14.8 1.0 O B:VAL241 4.5 19.9 1.0 CG B:GLU243 4.5 14.6 1.0 NE1 B:TRP176 4.6 17.0 1.0 O B:TRP179 4.6 13.3 1.0 O B:PRO238 4.7 18.4 1.0 CE2 B:TRP176 4.8 15.9 1.0 CA B:ASN178 5.0 14.2 1.0

A.Saaret, B.Villiers, F.Stricher, M.Anissimova, M.Cadillon, R.Spiess, S.Hay, D.Leys. Directed Evolution of Prenylated Fmn-Dependent Fdc Supports Efficient in Vivo Isobutene Production Nat Commun 2021.
ISSN: ESSN 2041-1723