Manganese in PDB 6evb: Structure of E282Q A. Niger FDC1 with Prfmn in the Iminium Form

All present enzymatic activity of Structure of E282Q A. Niger FDC1 with Prfmn in the Iminium Form:
4.1.1.102;

The structure of Structure of E282Q A. Niger FDC1 with Prfmn in the Iminium Form, PDB code: 6evb was solved by S.S.Bailey, D.Leys, K.A.P.Payne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.99 / 1.13
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	95.990, 63.920, 87.460, 90.00, 90.00, 90.00
R / Rfree (%)	14.3 / 15.7

The structure of Structure of E282Q A. Niger FDC1 with Prfmn in the Iminium Form also contains other interesting chemical elements:

Potassium

(K)

2 atoms

The binding sites of Manganese atom in the Structure of E282Q A. Niger FDC1 with Prfmn in the Iminium Form (pdb code 6evb). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Structure of E282Q A. Niger FDC1 with Prfmn in the Iminium Form, PDB code: 6evb:

Manganese binding site 1 out of 1 in the Structure of E282Q A. Niger FDC1 with Prfmn in the Iminium Form


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of E282Q A. Niger FDC1 with Prfmn in the Iminium Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn602 b:7.5 occ:1.00 OE2 A:GLU233 2.1 7.0 1.0 OD1 A:ASN168 2.2 7.3 1.0 O2P A:4LU601 2.2 6.6 1.0 O A:HOH760 2.2 7.7 1.0 O A:HOH850 2.2 8.3 1.0 ND1 A:HIS191 2.3 7.6 1.0 CG A:ASN168 3.1 7.0 1.0 CD A:GLU233 3.2 6.9 1.0 CE1 A:HIS191 3.2 7.6 1.0 P A:4LU601 3.4 6.7 1.0 CG A:HIS191 3.4 7.1 1.0 ND2 A:ASN168 3.5 7.2 1.0 OE1 A:GLU233 3.5 7.4 1.0 O3P A:4LU601 3.6 7.8 1.0 K A:K603 3.7 7.5 1.0 CB A:HIS191 3.8 7.5 1.0 O1P A:4LU601 4.3 7.7 1.0 CZ2 A:TRP166 4.3 9.0 1.0 O A:ILE227 4.4 7.6 1.0 NE2 A:HIS191 4.4 8.1 1.0 CG1 A:ILE227 4.4 8.4 1.0 CD2 A:HIS191 4.5 8.3 1.0 CB A:ASN168 4.5 7.4 1.0 O A:VAL231 4.5 8.4 1.0 O5' A:4LU601 4.5 7.1 1.0 CG A:GLU233 4.5 7.0 1.0 O A:TRP169 4.6 6.9 1.0 NE1 A:TRP166 4.6 8.6 1.0 O A:PRO228 4.7 8.2 1.0 CE2 A:TRP166 4.9 7.8 1.0 CA A:ASN168 5.0 7.0 1.0

S.S.Bailey, K.A.P.Payne, K.Fisher, S.A.Marshall, M.J.Cliff, R.Spiess, D.A.Parker, S.E.J.Rigby, D.Leys. The Role of Conserved Residues in Fdc Decarboxylase in Prenylated Flavin Mononucleotide Oxidative Maturation, Cofactor Isomerization, and Catalysis. J. Biol. Chem. V. 293 2272 2018.
ISSN: ESSN 1083-351X
PubMed: 29259125
DOI: 10.1074/JBC.RA117.000881