Manganese in PDB 7nf1: Structure of T. Atroviride Variant Tafdcv in Complex with Prfmn- Butynoic Acid Adduct

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

The structure of Structure of T. Atroviride Variant Tafdcv in Complex with Prfmn- Butynoic Acid Adduct, PDB code: 7nf1 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)	64.65 / 1.77
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	74.647, 74.647, 345.752, 90, 90, 120
R / Rfree (%)	17.5 / 20.6

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

Potassium

(K)

7 atoms

The binding sites of Manganese atom in the Structure of T. Atroviride Variant Tafdcv in Complex with Prfmn- Butynoic Acid Adduct (pdb code 7nf1). 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 Variant Tafdcv in Complex with Prfmn- Butynoic Acid Adduct, PDB code: 7nf1:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Structure of T. Atroviride Variant Tafdcv in Complex with Prfmn- Butynoic 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 Variant Tafdcv in Complex with Prfmn- Butynoic Acid Adduct within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn605 b:21.1 occ:1.00 ND2 A:ASN178 2.2 12.4 1.0 OE2 A:GLU243 2.2 15.9 1.0 O A:HOH763 2.2 12.7 1.0 O9 A:JRK601 2.2 15.8 1.0 O A:HOH792 2.3 16.6 1.0 ND1 A:HIS201 2.4 13.1 1.0 CG A:ASN178 3.2 13.0 1.0 CD A:GLU243 3.2 17.4 1.0 CE1 A:HIS201 3.3 14.8 1.0 P1 A:JRK601 3.4 16.1 1.0 CG A:HIS201 3.5 14.2 1.0 OD1 A:ASN178 3.5 17.4 1.0 OE1 A:GLU243 3.5 16.7 1.0 O7 A:JRK601 3.6 16.7 1.0 K A:K603 3.7 15.8 1.0 CB A:HIS201 3.8 15.6 1.0 O A:ILE237 4.3 17.4 1.0 CG1 A:ILE237 4.3 18.5 1.0 O8 A:JRK601 4.3 18.2 1.0 CZ2 A:TRP176 4.4 19.4 1.0 O6 A:JRK601 4.5 17.4 1.0 NE2 A:HIS201 4.5 15.9 1.0 CB A:ASN178 4.5 14.7 1.0 O A:VAL241 4.5 17.8 1.0 CD2 A:HIS201 4.6 14.8 1.0 CG A:GLU243 4.6 17.2 1.0 O A:TRP179 4.6 13.7 1.0 O A:PRO238 4.7 21.1 1.0 NE1 A:TRP176 4.8 19.5 1.0 CE2 A:TRP176 5.0 19.5 1.0

Manganese binding site 2 out of 2 in the Structure of T. Atroviride Variant Tafdcv in Complex with Prfmn- Butynoic 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 Variant Tafdcv in Complex with Prfmn- Butynoic Acid Adduct within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn606 b:24.2 occ:1.00 ND2 B:ASN178 2.2 14.6 1.0 OE2 B:GLU243 2.2 21.4 1.0 O8 B:JRK601 2.2 20.4 1.0 O B:HOH733 2.2 17.2 1.0 O B:HOH756 2.3 19.4 1.0 ND1 B:HIS201 2.3 18.6 1.0 CE1 B:HIS201 3.2 20.8 1.0 CG B:ASN178 3.2 18.4 1.0 CD B:GLU243 3.2 21.5 1.0 P1 B:JRK601 3.4 19.6 1.0 CG B:HIS201 3.4 18.9 1.0 OD1 B:ASN178 3.5 22.2 1.0 OE1 B:GLU243 3.5 22.1 1.0 O9 B:JRK601 3.6 21.3 1.0 K B:K605 3.7 20.8 1.0 CB B:HIS201 3.8 18.0 1.0 O7 B:JRK601 4.3 17.6 1.0 O B:ILE237 4.3 20.8 1.0 CG1 B:ILE237 4.3 22.7 1.0 CZ2 B:TRP176 4.3 24.5 1.0 NE2 B:HIS201 4.4 20.1 1.0 O6 B:JRK601 4.5 19.0 1.0 CB B:ASN178 4.5 17.2 1.0 O B:VAL241 4.5 23.5 1.0 CD2 B:HIS201 4.5 20.3 1.0 CG B:GLU243 4.6 21.5 1.0 NE1 B:TRP176 4.6 21.8 1.0 O B:TRP179 4.7 18.2 1.0 O B:PRO238 4.7 25.8 1.0 CE2 B:TRP176 4.9 21.6 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