Potassium in PDB 4za4: Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium Form.

All present enzymatic activity of Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium Form.:
4.1.1.61;

The structure of Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium Form., PDB code: 4za4 was solved by K.A.P.Payne, D.Leys, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.82 / 1.22
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	95.990, 63.930, 87.630, 90.00, 90.00, 90.00
R / Rfree (%)	14.6 / 16.1

The structure of Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium Form. also contains other interesting chemical elements:

Manganese

(Mn)

1 atom

The binding sites of Potassium atom in the Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium Form. (pdb code 4za4). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium Form., PDB code: 4za4:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium Form.


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium Form. within 5.0Å range: probe atom residue distance (Å) B Occ A:K603 b:7.7 occ:1.00 OE2 A:GLU233 2.8 7.5 1.0 O A:MET225 2.8 7.6 1.0 O A:ALA222 2.8 7.7 1.0 O2P A:4LU601 2.8 6.8 1.0 O5' A:4LU601 3.0 7.0 1.0 O A:TRP169 3.1 6.7 1.0 O A:SER223 3.1 8.9 1.0 O A:HOH727 3.3 7.6 1.0 P A:4LU601 3.4 6.6 1.0 C A:SER223 3.5 7.2 1.0 O3P A:4LU601 3.6 7.3 1.0 CD A:GLU233 3.6 7.2 1.0 MN A:MN602 3.7 7.3 1.0 CA A:SER223 3.7 7.2 1.0 CG A:GLU233 3.8 7.8 1.0 C A:ALA222 3.9 7.0 1.0 C A:MET225 3.9 7.5 1.0 N A:MET225 4.1 7.2 1.0 N A:SER223 4.2 6.7 1.0 C5' A:4LU601 4.3 6.8 1.0 C A:TRP169 4.3 6.4 1.0 N A:SER224 4.3 6.8 0.5 O4' A:4LU601 4.3 8.2 1.0 C4' A:4LU601 4.3 7.7 1.0 N A:SER224 4.4 6.8 0.5 CB A:SER170 4.4 7.0 1.0 CA A:SER170 4.5 6.7 1.0 CA A:MET225 4.5 7.1 1.0 OE1 A:GLU233 4.7 7.6 1.0 C A:SER224 4.8 7.4 0.5 C A:SER224 4.8 7.3 0.5 ND2 A:ASN168 4.9 7.5 1.0 O1P A:4LU601 4.9 7.7 1.0 N A:SER170 4.9 6.5 1.0 N A:PRO226 4.9 7.2 1.0 N A:ILE227 4.9 7.4 1.0 CG1 A:ILE227 4.9 9.4 1.0 CA A:SER224 5.0 6.5 0.5 CB A:SER223 5.0 6.6 1.0 CA A:SER224 5.0 6.6 0.5

Potassium binding site 2 out of 2 in the Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium Form.


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium Form. within 5.0Å range: probe atom residue distance (Å) B Occ A:K604 b:8.2 occ:1.00 O A:ARG421 2.7 8.1 1.0 O A:LEU461 2.7 9.4 1.0 O A:ASP459 2.7 7.9 1.0 OD2 A:ASP427 2.8 9.1 1.0 CG A:ASP427 3.4 8.9 1.0 C A:ASP459 3.7 7.1 1.0 C A:LEU461 3.8 8.0 1.0 C A:ARG421 3.8 7.2 1.0 CB A:ASP427 3.9 8.0 1.0 CA A:CYS422 4.1 7.4 1.0 OD1 A:ASP427 4.1 9.8 1.0 N A:LEU461 4.2 7.8 1.0 CA A:ALA460 4.3 7.5 1.0 C A:ALA460 4.4 7.5 1.0 N A:CYS422 4.4 7.2 1.0 N A:ALA460 4.4 7.2 1.0 CG A:ASP459 4.5 10.1 1.0 CB A:ASP459 4.5 8.3 1.0 CA A:LEU461 4.6 8.0 1.0 N A:MET462 4.6 8.5 1.0 CA A:MET462 4.7 8.2 1.0 N A:ARG423 4.8 7.0 1.0 OD2 A:ASP459 4.8 14.9 1.0 OD1 A:ASP459 4.8 10.2 1.0 CA A:ASP459 4.8 7.2 1.0 CA A:ARG421 4.9 7.0 1.0

K.A.Payne, M.D.White, K.Fisher, B.Khara, S.S.Bailey, D.Parker, N.J.Rattray, D.K.Trivedi, R.Goodacre, R.Beveridge, P.Barran, S.E.Rigby, N.S.Scrutton, S.Hay, D.Leys. New Cofactor Supports Alpha , Beta-Unsaturated Acid Decarboxylation Via 1,3-Dipolar Cycloaddition. Nature V. 522 502 2015.
ISSN: ESSN 1476-4687
PubMed: 26083754
DOI: 10.1038/NATURE14560