Manganese in PDB 6da9: Crystal Structure of the Ttnd Decarboxylase From the Tautomycetin Biosynthesis Pathway of Streptomyces Griseochromogenes with Fmn Bound at 2.05 A Resolution

The structure of Crystal Structure of the Ttnd Decarboxylase From the Tautomycetin Biosynthesis Pathway of Streptomyces Griseochromogenes with Fmn Bound at 2.05 A Resolution, PDB code: 6da9 was solved by L.Han, J.D.Rudolf, C.-Y.Chang, M.D.Miller, J.Soman, W.Xu, G.N.Phillips Jr., B.Shen, Enzyme Discovery For Natural Product Biosynthesis (Natpro), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.98 / 2.05
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	52.070, 116.109, 193.969, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 21.6

The binding sites of Manganese atom in the Crystal Structure of the Ttnd Decarboxylase From the Tautomycetin Biosynthesis Pathway of Streptomyces Griseochromogenes with Fmn Bound at 2.05 A Resolution (pdb code 6da9). 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 Crystal Structure of the Ttnd Decarboxylase From the Tautomycetin Biosynthesis Pathway of Streptomyces Griseochromogenes with Fmn Bound at 2.05 A Resolution, PDB code: 6da9:

Manganese binding site 1 out of 1 in the Crystal Structure of the Ttnd Decarboxylase From the Tautomycetin Biosynthesis Pathway of Streptomyces Griseochromogenes with Fmn Bound at 2.05 A Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of the Ttnd Decarboxylase From the Tautomycetin Biosynthesis Pathway of Streptomyces Griseochromogenes with Fmn Bound at 2.05 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn502 b:43.5 occ:1.00 OD1 A:ASN164 2.0 48.0 1.0 O A:HOH625 2.0 35.6 1.0 O1P A:FMN501 2.1 42.7 1.0 ND1 A:HIS187 2.2 44.1 1.0 O A:HOH602 2.3 48.2 1.0 OE2 A:GLU228 2.3 42.0 1.0 CG A:ASN164 3.1 49.0 1.0 CE1 A:HIS187 3.1 42.6 1.0 CD A:GLU228 3.3 53.6 1.0 CG A:HIS187 3.3 42.4 1.0 P A:FMN501 3.3 42.2 1.0 OE1 A:GLU228 3.6 37.7 1.0 ND2 A:ASN164 3.6 37.1 1.0 O3P A:FMN501 3.7 40.7 1.0 CB A:HIS187 3.7 39.2 1.0 O A:HOH617 3.9 29.4 1.0 O2P A:FMN501 4.2 41.7 1.0 NE2 A:HIS187 4.3 42.8 1.0 CB A:ASN164 4.3 39.8 1.0 CD2 A:HIS187 4.4 43.0 1.0 O5' A:FMN501 4.5 44.4 1.0 O A:ILE226 4.6 53.9 1.0 O A:TRP165 4.7 41.2 1.0 CG A:GLU228 4.7 42.8 1.0 O A:LEU222 4.8 40.1 1.0 CA A:ASN164 4.9 44.8 1.0

T.Annaval, L.Han, J.D.Rudolf, G.Xie, D.Yang, C.Y.Chang, M.Ma, I.Crnovcic, M.D.Miller, J.Soman, W.Xu, G.N.Phillips Jr., B.Shen. Biochemical and Structural Characterization of Ttnd, A Prenylated Fmn-Dependent Decarboxylase From the Tautomycetin Biosynthetic Pathway. Acs Chem. Biol. V. 13 2728 2018.
ISSN: ESSN 1554-8937
PubMed: 30152678
DOI: 10.1021/ACSCHEMBIO.8B00673