Manganese in PDB 4za5: Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium and Ketimine Forms.

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

The structure of Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium and Ketimine Forms., PDB code: 4za5 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)	48.01 / 1.10
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	96.020, 63.790, 87.720, 90.00, 90.00, 90.00
R / Rfree (%)	14.4 / 15.6

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

Potassium

(K)

3 atoms

The binding sites of Manganese atom in the Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium and Ketimine Forms. (pdb code 4za5). 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 A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium and Ketimine Forms., PDB code: 4za5:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium and Ketimine Forms.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium and Ketimine Forms. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn603 b:6.9 occ:0.60 MN A:MN603 0.0 6.9 0.6 MN A:MN603 0.4 8.8 0.4 O8 A:FZZ602 2.1 7.8 0.5 O2P A:4LU601 2.1 6.6 0.5 OD1 A:ASN168 2.1 7.5 1.0 OE2 A:GLU233 2.2 8.2 1.0 O A:HOH709 2.2 8.1 1.0 ND1 A:HIS191 2.2 8.3 1.0 O A:HOH821 2.3 8.7 1.0 CG A:ASN168 3.1 7.6 1.0 CE1 A:HIS191 3.1 8.2 1.0 CD A:GLU233 3.2 8.1 1.0 P1 A:FZZ602 3.2 7.4 0.5 CG A:HIS191 3.3 7.5 1.0 P A:4LU601 3.4 6.3 0.5 ND2 A:ASN168 3.5 8.1 1.0 O7 A:FZZ602 3.5 9.4 0.5 O3P A:4LU601 3.6 7.9 0.5 OE1 A:GLU233 3.6 8.2 1.0 K A:K604 3.6 10.9 0.4 CB A:HIS191 3.7 8.1 1.0 K A:K604 3.7 6.4 0.6 O6 A:FZZ602 4.2 7.3 0.5 O9 A:FZZ602 4.2 8.0 0.5 O1P A:4LU601 4.3 8.8 0.5 CZ2 A:TRP166 4.3 9.3 1.0 NE2 A:HIS191 4.4 9.1 1.0 O A:ILE227 4.4 8.4 1.0 CB A:ASN168 4.4 7.6 1.0 CD2 A:HIS191 4.4 8.5 1.0 O5' A:4LU601 4.5 6.3 0.5 CG1 A:ILE227 4.5 10.2 1.0 O A:VAL231 4.5 9.4 1.0 CG A:GLU233 4.5 8.2 1.0 O A:TRP169 4.6 7.2 1.0 NE1 A:TRP166 4.6 9.9 1.0 O A:PRO228 4.8 9.4 1.0 CE2 A:TRP166 4.8 9.1 1.0 CA A:ASN168 5.0 7.1 1.0

Manganese binding site 2 out of 2 in the Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium and Ketimine Forms.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of A. Niger FDC1 with the Prenylated-Flavin Cofactor in the Iminium and Ketimine Forms. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn603 b:8.8 occ:0.40 MN A:MN603 0.0 8.8 0.4 MN A:MN603 0.4 6.9 0.6 O A:HOH821 1.9 8.7 1.0 OE2 A:GLU233 2.0 8.2 1.0 O A:HOH709 2.1 8.1 1.0 OD1 A:ASN168 2.3 7.5 1.0 ND1 A:HIS191 2.4 8.3 1.0 O8 A:FZZ602 2.4 7.8 0.5 O2P A:4LU601 2.5 6.6 0.5 CD A:GLU233 3.0 8.1 1.0 CE1 A:HIS191 3.2 8.2 1.0 CG A:ASN168 3.3 7.6 1.0 OE1 A:GLU233 3.5 8.2 1.0 P1 A:FZZ602 3.6 7.4 0.5 CG A:HIS191 3.6 7.5 1.0 K A:K604 3.6 10.9 0.4 O7 A:FZZ602 3.7 9.4 0.5 P A:4LU601 3.7 6.3 0.5 K A:K604 3.7 6.4 0.6 O3P A:4LU601 3.8 7.9 0.5 ND2 A:ASN168 3.8 8.1 1.0 CB A:HIS191 4.0 8.1 1.0 CG1 A:ILE227 4.1 10.2 1.0 O A:ILE227 4.1 8.4 1.0 O A:VAL231 4.2 9.4 1.0 CG A:GLU233 4.3 8.2 1.0 CZ2 A:TRP166 4.4 9.3 1.0 O6 A:FZZ602 4.4 7.3 0.5 NE2 A:HIS191 4.5 9.1 1.0 O A:PRO228 4.5 9.4 1.0 NE1 A:TRP166 4.5 9.9 1.0 O9 A:FZZ602 4.6 8.0 0.5 CB A:ASN168 4.6 7.6 1.0 CD2 A:HIS191 4.6 8.5 1.0 O1P A:4LU601 4.7 8.8 0.5 O A:TRP169 4.7 7.2 1.0 O5' A:4LU601 4.7 6.3 0.5 CD1 A:ILE227 4.8 10.5 1.0 CE2 A:TRP166 4.8 9.1 1.0 C A:ILE227 4.9 8.8 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